Iron in PDB 7xqw: Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)

All present enzymatic activity of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1):
1.17.1.9; 1.2.1.2;

The structure of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) also contains other interesting chemical elements:

Tungsten

(W)

1 atom

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Iron atom in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) (pdb code 7xqw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1), PDB code: 7xqw:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1004 b:11.8 occ:1.00 FE1 A:FES1004 0.0 11.8 1.0 S1 A:FES1004 2.2 11.8 1.0 S2 A:FES1004 2.2 11.8 1.0 SG A:CYS102 2.3 6.0 1.0 N A:HIS103 2.3 6.2 1.0 SG A:CYS115 2.4 5.2 1.0 N A:CYS102 2.6 6.0 1.0 FE2 A:FES1004 2.7 11.8 1.0 CA A:CYS102 3.0 6.0 1.0 C A:CYS102 3.0 6.0 1.0 CB A:CYS102 3.1 6.0 1.0 N A:LEU101 3.4 5.1 1.0 CA A:HIS103 3.4 6.2 1.0 CB A:HIS103 3.4 6.2 1.0 C A:LEU101 3.5 5.1 1.0 CB A:CYS115 3.9 5.2 1.0 SG A:CYS132 4.0 6.7 1.0 CA A:LEU101 4.0 5.1 1.0 C A:HIS100 4.2 5.7 1.0 O A:CYS102 4.2 6.0 1.0 CA A:HIS100 4.2 5.7 1.0 CB A:HIS100 4.3 5.7 1.0 SG A:CYS118 4.4 6.4 1.0 O A:LEU101 4.4 5.1 1.0 C A:HIS103 4.5 6.2 1.0 O A:ASP112 4.5 6.1 1.0 CB A:CYS132 4.5 6.7 1.0 O A:HIS103 4.6 6.2 1.0 CB A:LEU101 4.7 5.1 1.0 CG A:HIS103 4.9 6.2 1.0 CB A:CYS118 4.9 6.4 1.0 CA A:CYS115 5.0 5.2 1.0 N A:CYS115 5.0 5.2 1.0

Iron binding site 2 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1004 b:11.8 occ:1.00 FE2 A:FES1004 0.0 11.8 1.0 CB A:CYS132 2.1 6.7 1.0 S2 A:FES1004 2.2 11.8 1.0 S1 A:FES1004 2.2 11.8 1.0 SG A:CYS118 2.3 6.4 1.0 SG A:CYS132 2.3 6.7 1.0 FE1 A:FES1004 2.7 11.8 1.0 SG A:CYS102 3.0 6.0 1.0 CA A:CYS132 3.5 6.7 1.0 CB A:CYS118 3.6 6.4 1.0 SG A:CYS115 3.6 5.2 1.0 O A:ASP112 4.0 6.1 1.0 CB A:HIS103 4.0 6.2 1.0 CA A:GLY113 4.1 6.3 1.0 N A:CYS132 4.2 6.7 1.0 N A:HIS103 4.2 6.2 1.0 C A:CYS132 4.6 6.7 1.0 N A:CYS118 4.6 6.4 1.0 CA A:HIS103 4.7 6.2 1.0 CB A:ALA130 4.7 7.4 1.0 C A:ASP112 4.7 6.1 1.0 CB A:CYS102 4.7 6.0 1.0 CA A:CYS118 4.8 6.4 1.0 N A:GLY113 4.9 6.3 1.0 C A:GLY113 4.9 6.3 1.0 N A:ARG116 5.0 5.8 1.0 C A:CYS102 5.0 6.0 1.0

Iron binding site 3 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1005 b:5.7 occ:1.00 FE1 A:SF41005 0.0 5.7 1.0 SG A:CYS216 2.3 5.0 1.0 S3 A:SF41005 2.3 5.7 1.0 S2 A:SF41005 2.3 5.7 1.0 S4 A:SF41005 2.3 5.7 1.0 FE4 A:SF41005 2.7 5.7 1.0 FE3 A:SF41005 2.7 5.7 1.0 FE2 A:SF41005 2.7 5.7 1.0 N A:CYS216 3.5 5.0 1.0 CB A:CYS216 3.6 5.0 1.0 N A:ASN217 3.8 5.4 1.0 S1 A:SF41005 3.9 5.7 1.0 CD A:PRO267 3.9 4.4 1.0 CA A:CYS216 3.9 5.0 1.0 C A:CYS216 4.1 5.0 1.0 N A:LEU218 4.2 5.1 1.0 N A:GLN215 4.4 5.3 1.0 C A:GLN215 4.5 5.3 1.0 CG A:PRO267 4.5 4.4 1.0 SG A:CYS266 4.7 4.5 1.0 SG A:CYS219 4.7 4.8 1.0 CB A:LEU218 4.7 5.1 1.0 N A:ILE214 4.7 4.9 1.0 CA A:GLN215 4.7 5.3 1.0 SG A:CYS213 4.7 4.7 1.0 CA A:ASN217 4.8 5.4 1.0 N A:CYS219 4.8 4.8 1.0 C A:ASN217 4.9 5.4 1.0 CB A:ILE214 5.0 4.9 1.0 CA A:LEU218 5.0 5.1 1.0 C A:ILE214 5.0 4.9 1.0

Iron binding site 4 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1005 b:5.7 occ:1.00 FE2 A:SF41005 0.0 5.7 1.0 SG A:CYS213 2.3 4.7 1.0 S4 A:SF41005 2.3 5.7 1.0 S1 A:SF41005 2.3 5.7 1.0 S3 A:SF41005 2.3 5.7 1.0 FE3 A:SF41005 2.7 5.7 1.0 FE4 A:SF41005 2.7 5.7 1.0 FE1 A:SF41005 2.7 5.7 1.0 CB A:CYS213 3.4 4.7 1.0 N A:ILE214 3.6 4.9 1.0 CA A:CYS213 3.7 4.7 1.0 N A:GLN215 3.8 5.3 1.0 S2 A:SF41005 3.9 5.7 1.0 CG2 A:VAL243 4.0 6.2 1.0 C A:CYS213 4.1 4.7 1.0 CA A:GLN215 4.4 5.3 1.0 CB A:ALA270 4.5 4.9 1.0 N A:CYS216 4.6 5.0 1.0 CA A:ILE214 4.7 4.9 1.0 C A:ILE214 4.7 4.9 1.0 SG A:CYS219 4.7 4.8 1.0 SG A:CYS266 4.8 4.5 1.0 SG A:CYS216 4.9 5.0 1.0

Iron binding site 5 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1005 b:5.7 occ:1.00 FE3 A:SF41005 0.0 5.7 1.0 SG A:CYS266 2.3 4.5 1.0 S1 A:SF41005 2.3 5.7 1.0 S4 A:SF41005 2.3 5.7 1.0 S2 A:SF41005 2.3 5.7 1.0 FE2 A:SF41005 2.7 5.7 1.0 FE1 A:SF41005 2.7 5.7 1.0 FE4 A:SF41005 2.7 5.7 1.0 CB A:CYS266 3.4 4.5 1.0 CA A:CYS266 3.8 4.5 1.0 S3 A:SF41005 3.9 5.7 1.0 CD A:PRO267 4.0 4.4 1.0 CB A:ALA270 4.0 4.9 1.0 OG1 A:THR268 4.0 4.7 1.0 SG A:CYS216 4.6 5.0 1.0 N A:PRO267 4.6 4.4 1.0 C A:CYS266 4.6 4.5 1.0 CG A:LEU271 4.7 5.1 1.0 CD1 A:LEU271 4.7 5.1 1.0 N A:LEU271 4.8 5.1 1.0 SG A:CYS219 4.9 4.8 1.0 SG A:CYS213 4.9 4.7 1.0 N A:THR268 4.9 4.7 1.0 N A:CYS266 5.0 4.5 1.0

Iron binding site 6 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1005 b:5.7 occ:1.00 FE4 A:SF41005 0.0 5.7 1.0 SG A:CYS219 2.3 4.8 1.0 S2 A:SF41005 2.3 5.7 1.0 S3 A:SF41005 2.3 5.7 1.0 S1 A:SF41005 2.3 5.7 1.0 FE1 A:SF41005 2.7 5.7 1.0 FE2 A:SF41005 2.7 5.7 1.0 FE3 A:SF41005 2.7 5.7 1.0 CB A:CYS219 3.2 4.8 1.0 N A:CYS219 3.8 4.8 1.0 S4 A:SF41005 3.9 5.7 1.0 CG2 A:VAL243 3.9 6.2 1.0 CA A:CYS219 4.1 4.8 1.0 CD1 A:LEU271 4.6 5.1 1.0 SG A:CYS213 4.6 4.7 1.0 N A:LEU218 4.7 5.1 1.0 SG A:CYS216 4.8 5.0 1.0 N A:ASN217 4.8 5.4 1.0 SG A:CYS266 4.8 4.5 1.0 CG1 A:VAL243 4.8 6.2 1.0 C A:LEU218 4.9 5.1 1.0 CB A:VAL243 4.9 6.2 1.0 C A:ASN217 5.0 5.4 1.0

Iron binding site 7 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1006 b:5.8 occ:1.00 FE1 A:SF41006 0.0 5.8 1.0 SG A:CYS262 2.3 4.5 1.0 S4 A:SF41006 2.3 5.8 1.0 S3 A:SF41006 2.3 5.8 1.0 S2 A:SF41006 2.3 5.8 1.0 FE2 A:SF41006 2.7 5.8 1.0 FE4 A:SF41006 2.7 5.8 1.0 FE3 A:SF41006 2.7 5.8 1.0 CB A:CYS262 3.2 4.5 1.0 N A:CYS262 3.7 4.5 1.0 S1 A:SF41006 3.9 5.8 1.0 CA A:CYS262 4.1 4.5 1.0 CD1 A:ILE232 4.2 6.5 1.0 CE A:MET251 4.3 8.1 1.0 N A:GLU261 4.5 5.2 1.0 SG A:CYS256 4.7 7.9 1.0 SG A:CYS223 4.7 5.7 1.0 N A:GLY260 4.8 4.6 1.0 SG A:CYS259 4.8 4.9 1.0 CB A:CYS223 4.9 5.7 1.0 C A:GLU261 4.9 5.2 1.0 N A:VAL263 4.9 4.8 1.0 C A:GLY260 4.9 4.6 1.0 CA A:GLY260 4.9 4.6 1.0

Iron binding site 8 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1006 b:5.8 occ:1.00 FE2 A:SF41006 0.0 5.8 1.0 SG A:CYS256 2.3 7.9 1.0 S3 A:SF41006 2.3 5.8 1.0 S4 A:SF41006 2.3 5.8 1.0 S1 A:SF41006 2.3 5.8 1.0 FE1 A:SF41006 2.7 5.8 1.0 FE3 A:SF41006 2.7 5.8 1.0 FE4 A:SF41006 2.7 5.8 1.0 CB A:CYS256 3.5 7.9 1.0 CE A:MET251 3.8 8.1 1.0 S2 A:SF41006 3.9 5.8 1.0 CA A:CYS256 3.9 7.9 1.0 N A:ALA258 3.9 5.5 1.0 N A:VAL257 4.0 6.4 1.0 CE A:MET206 4.2 6.6 1.0 C A:CYS256 4.4 7.9 1.0 CA A:ALA258 4.4 5.5 1.0 SG A:CYS262 4.7 4.5 1.0 N A:CYS259 4.7 4.9 1.0 SG A:CYS259 4.8 4.9 1.0 SG A:CYS223 4.8 5.7 1.0 C A:VAL257 4.9 6.4 1.0

Iron binding site 9 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1006 b:5.8 occ:1.00 FE3 A:SF41006 0.0 5.8 1.0 SG A:CYS259 2.3 4.9 1.0 S2 A:SF41006 2.3 5.8 1.0 S1 A:SF41006 2.3 5.8 1.0 S4 A:SF41006 2.3 5.8 1.0 FE4 A:SF41006 2.7 5.8 1.0 FE2 A:SF41006 2.7 5.8 1.0 FE1 A:SF41006 2.7 5.8 1.0 N A:CYS259 3.7 4.9 1.0 CB A:CYS259 3.8 4.9 1.0 N A:GLY260 3.8 4.6 1.0 S3 A:SF41006 3.9 5.8 1.0 N A:GLU261 4.1 5.2 1.0 CA A:CYS259 4.1 4.9 1.0 OD1 A:ASN229 4.2 7.0 1.0 C A:CYS259 4.3 4.9 1.0 N A:ALA258 4.6 5.5 1.0 CG2 A:VAL257 4.6 6.4 1.0 C A:ALA258 4.6 5.5 1.0 CB A:GLU261 4.6 5.2 1.0 SG A:CYS223 4.7 5.7 1.0 CA A:GLY260 4.7 4.6 1.0 SG A:CYS256 4.8 7.9 1.0 SG A:CYS262 4.8 4.5 1.0 N A:CYS262 4.8 4.5 1.0 CG A:ASN229 4.9 7.0 1.0 C A:GLY260 4.9 4.6 1.0 CA A:ALA258 4.9 5.5 1.0 CA A:GLU261 4.9 5.2 1.0

Iron binding site 10 out of 20 in the Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Formate Dehydrogenase (Fdh) From Methylobacterium Extorquens AM1 (MEFDH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1006 b:5.8 occ:1.00 FE4 A:SF41006 0.0 5.8 1.0 SG A:CYS223 2.3 5.7 1.0 S2 A:SF41006 2.3 5.8 1.0 S3 A:SF41006 2.3 5.8 1.0 S1 A:SF41006 2.3 5.8 1.0 FE3 A:SF41006 2.7 5.8 1.0 FE1 A:SF41006 2.7 5.8 1.0 FE2 A:SF41006 2.7 5.8 1.0 CB A:CYS223 3.2 5.7 1.0 S4 A:SF41006 3.9 5.8 1.0 CA A:CYS223 3.9 5.7 1.0 CB A:VAL231 4.2 7.9 1.0 CB A:ASN229 4.4 7.0 1.0 CD1 A:ILE232 4.4 6.5 1.0 CG1 A:ILE232 4.5 6.5 1.0 SG A:CYS259 4.7 4.9 1.0 OD1 A:ASN229 4.8 7.0 1.0 CG2 A:VAL231 4.8 7.9 1.0 SG A:CYS256 4.8 7.9 1.0 SG A:CYS262 4.8 4.5 1.0 N A:CYS223 4.9 5.7 1.0 N A:VAL231 4.9 7.9 1.0 C A:VAL231 4.9 7.9 1.0 CA A:VAL231 4.9 7.9 1.0 O A:VAL231 4.9 7.9 1.0 C A:CYS223 5.0 5.7 1.0

B.W.Jeon, Y.Y.Heo, J.Park, S.H.Roh, H.H.Lee, Y.H.Kim. Enzymatic Conversion of CO2 in Real Flue Gas to Molar-Scale Formate To Be Published.