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Iron in PDB 8h2t: Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa (pdb code 8h2t). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 9 binding sites of Iron where determined in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa, PDB code: 8h2t:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Iron binding site 1 out of 9 in 8h2t

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Iron binding site 1 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


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Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:111.4
occ:1.00
FE1 B:FES501 0.0 111.4 1.0
ND1 B:HIS87 2.1 79.6 1.0
ND1 B:HIS109 2.1 79.0 1.0
S1 B:FES501 2.2 105.8 1.0
S2 B:FES501 2.2 104.8 1.0
FE2 B:FES501 2.7 126.3 1.0
CG B:HIS87 2.9 85.1 1.0
CE1 B:HIS109 2.9 88.7 1.0
CB B:HIS87 3.0 85.7 1.0
CG B:HIS109 3.2 85.2 1.0
CE1 B:HIS87 3.2 82.8 1.0
CB B:HIS109 3.6 88.8 1.0
NE2 B:HIS109 4.1 84.9 1.0
N B:HIS109 4.1 83.2 1.0
CD2 B:HIS87 4.1 79.2 1.0
CD2 B:HIS109 4.2 85.6 1.0
N B:LYS88 4.2 71.8 1.0
NE2 B:HIS87 4.2 86.2 1.0
CB B:TYR108 4.3 80.8 1.0
CA B:HIS87 4.3 77.6 1.0
SG B:CYS85 4.4 77.2 1.0
CA B:HIS109 4.4 87.0 1.0
CD2 B:TYR108 4.4 83.2 1.0
SG B:CYS106 4.5 86.2 1.0
CB B:LYS88 4.6 79.5 1.0
C B:HIS87 4.6 81.0 1.0
CG B:LYS88 4.6 80.9 1.0
CG B:TYR108 4.7 88.0 1.0
CD1 B:TRP111 4.7 74.6 1.0
NE1 B:TRP111 4.9 78.3 1.0
C B:TYR108 4.9 79.6 1.0
CG B:TRP111 5.0 71.3 1.0

Iron binding site 2 out of 9 in 8h2t

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Iron binding site 2 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:126.3
occ:1.00
FE2 B:FES501 0.0 126.3 1.0
S1 B:FES501 2.2 105.8 1.0
S2 B:FES501 2.2 104.8 1.0
SG B:CYS106 2.3 86.2 1.0
SG B:CYS85 2.3 77.2 1.0
FE1 B:FES501 2.7 111.4 1.0
CB B:CYS85 3.1 65.8 1.0
CB B:CYS106 3.2 80.1 1.0
CB B:HIS87 3.8 85.7 1.0
CB B:TYR108 4.5 80.8 1.0
ND1 B:HIS87 4.5 79.6 1.0
CA B:CYS85 4.5 78.3 1.0
N B:HIS87 4.5 80.6 1.0
N B:LYS88 4.6 71.8 1.0
CG B:HIS87 4.6 85.1 1.0
ND1 B:HIS109 4.6 79.0 1.0
CB B:SER90 4.6 84.2 1.0
CA B:CYS106 4.7 80.9 1.0
CB B:TRP111 4.7 72.3 1.0
N B:HIS109 4.7 83.2 1.0
CA B:HIS87 4.7 77.6 1.0
CG B:TRP111 4.9 71.3 1.0
N B:SER90 4.9 80.8 1.0
C B:CYS85 4.9 82.0 1.0
O B:SER90 5.0 96.6 1.0

Iron binding site 3 out of 9 in 8h2t

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Iron binding site 3 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe503

b:150.2
occ:1.00
OD2 B:ASP377 2.0 101.2 1.0
OD1 B:ASP377 2.1 101.1 1.0
NE2 B:HIS216 2.2 80.2 1.0
OD1 B:ASN210 2.3 102.4 1.0
CG B:ASP377 2.3 97.5 1.0
NE2 B:HIS221 2.7 92.8 1.0
CE1 B:HIS216 2.9 82.8 1.0
ND2 B:ASN210 2.9 99.2 1.0
CG B:ASN210 2.9 98.1 1.0
CD2 B:HIS216 3.0 77.7 1.0
CE1 B:HIS221 3.4 95.6 1.0
CB B:ASP377 3.8 89.6 1.0
ND1 B:HIS216 3.8 82.9 1.0
CD2 B:HIS221 3.9 94.6 1.0
CG B:HIS216 3.9 82.0 1.0
CB B:ASN210 4.4 94.0 1.0
ND1 B:HIS221 4.6 90.5 1.0
O B:ASN210 4.6 107.1 1.0
CA B:ASP377 4.7 88.9 1.0
OH B:TYR381 4.7 88.4 1.0
C8 B:IAC502 4.8 112.4 1.0
CG B:HIS221 4.9 90.1 1.0
N B:IAC502 4.9 112.0 1.0
C7 B:IAC502 5.0 116.0 1.0

Iron binding site 4 out of 9 in 8h2t

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Iron binding site 4 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:110.2
occ:1.00
FE1 D:FES501 0.0 110.2 1.0
ND1 D:HIS109 2.1 78.8 1.0
ND1 D:HIS87 2.1 82.4 1.0
S1 D:FES501 2.2 106.8 1.0
S2 D:FES501 2.2 103.1 1.0
FE2 D:FES501 2.7 123.0 1.0
CG D:HIS87 2.9 87.3 1.0
CE1 D:HIS109 2.9 88.0 1.0
CB D:HIS87 3.0 85.6 1.0
CG D:HIS109 3.2 86.0 1.0
CE1 D:HIS87 3.2 85.0 1.0
CB D:HIS109 3.7 86.6 1.0
NE2 D:HIS109 4.0 85.6 1.0
CD2 D:HIS87 4.1 82.4 1.0
N D:HIS109 4.1 81.3 1.0
CD2 D:HIS109 4.2 87.2 1.0
N D:LYS88 4.2 74.0 1.0
NE2 D:HIS87 4.2 88.2 1.0
CB D:TYR108 4.3 82.8 1.0
CA D:HIS87 4.3 79.7 1.0
SG D:CYS85 4.4 82.7 1.0
CD2 D:TYR108 4.4 84.3 1.0
SG D:CYS106 4.5 84.0 1.0
CA D:HIS109 4.5 82.4 1.0
CB D:LYS88 4.6 79.5 1.0
C D:HIS87 4.6 82.4 1.0
CG D:LYS88 4.6 81.4 1.0
CG D:TYR108 4.7 89.1 1.0
CD1 D:TRP111 4.8 75.0 1.0
NE1 D:TRP111 4.9 78.2 1.0
C D:TYR108 4.9 82.1 1.0
N D:HIS87 5.0 84.1 1.0

Iron binding site 5 out of 9 in 8h2t

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Iron binding site 5 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:123.0
occ:1.00
FE2 D:FES501 0.0 123.0 1.0
S1 D:FES501 2.2 106.8 1.0
S2 D:FES501 2.2 103.1 1.0
SG D:CYS106 2.3 84.0 1.0
SG D:CYS85 2.3 82.7 1.0
FE1 D:FES501 2.7 110.2 1.0
CB D:CYS85 3.1 68.4 1.0
CB D:CYS106 3.2 79.3 1.0
CB D:HIS87 3.8 85.6 1.0
CB D:TYR108 4.5 82.8 1.0
ND1 D:HIS87 4.5 82.4 1.0
N D:HIS87 4.5 84.1 1.0
CA D:CYS85 4.6 78.1 1.0
N D:LYS88 4.6 74.0 1.0
ND1 D:HIS109 4.6 78.8 1.0
CG D:HIS87 4.6 87.3 1.0
CA D:CYS106 4.6 80.0 1.0
CB D:TRP111 4.7 74.4 1.0
CB D:SER90 4.7 81.0 1.0
N D:HIS109 4.7 81.3 1.0
CA D:HIS87 4.7 79.7 1.0
CG D:TRP111 4.9 73.0 1.0
N D:SER90 4.9 73.9 1.0
C D:CYS85 5.0 81.9 1.0
O D:SER90 5.0 92.2 1.0

Iron binding site 6 out of 9 in 8h2t

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Iron binding site 6 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe503

b:154.4
occ:1.00
OD2 D:ASP377 2.0 98.8 1.0
OD1 D:ASP377 2.1 99.9 1.0
NE2 D:HIS216 2.2 84.8 1.0
OD1 D:ASN210 2.3 98.4 1.0
CG D:ASP377 2.3 95.8 1.0
NE2 D:HIS221 2.7 91.2 1.0
ND2 D:ASN210 2.9 98.2 1.0
CE1 D:HIS216 2.9 86.1 1.0
CG D:ASN210 2.9 94.5 1.0
CD2 D:HIS216 3.0 82.7 1.0
CE1 D:HIS221 3.4 93.6 1.0
CB D:ASP377 3.8 88.5 1.0
ND1 D:HIS216 3.9 86.7 1.0
CD2 D:HIS221 3.9 91.5 1.0
CG D:HIS216 3.9 83.7 1.0
CB D:ASN210 4.4 91.1 1.0
ND1 D:HIS221 4.6 86.9 1.0
O D:ASN210 4.7 104.3 1.0
CA D:ASP377 4.7 89.1 1.0
OH D:TYR381 4.7 94.7 1.0
C8 D:IAC502 4.7 111.5 1.0
N D:IAC502 4.8 111.0 1.0
CG D:HIS221 4.9 85.3 1.0

Iron binding site 7 out of 9 in 8h2t

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Iron binding site 7 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe501

b:110.5
occ:1.00
FE1 G:FES501 0.0 110.5 1.0
ND1 G:HIS87 2.1 79.1 1.0
ND1 G:HIS109 2.1 78.6 1.0
S1 G:FES501 2.2 101.7 1.0
S2 G:FES501 2.2 106.2 1.0
FE2 G:FES501 2.7 123.0 1.0
CE1 G:HIS109 2.9 88.1 1.0
CG G:HIS87 2.9 84.9 1.0
CB G:HIS87 3.0 84.3 1.0
CG G:HIS109 3.2 86.4 1.0
CE1 G:HIS87 3.2 81.7 1.0
CB G:HIS109 3.7 87.6 1.0
NE2 G:HIS109 4.0 84.2 1.0
N G:HIS109 4.1 82.1 1.0
CD2 G:HIS87 4.1 79.9 1.0
CD2 G:HIS109 4.2 86.4 1.0
N G:LYS88 4.2 75.7 1.0
CB G:TYR108 4.2 75.5 1.0
NE2 G:HIS87 4.2 84.7 1.0
CD2 G:TYR108 4.3 82.2 1.0
CA G:HIS87 4.4 78.2 1.0
SG G:CYS85 4.4 79.9 1.0
SG G:CYS106 4.5 85.4 1.0
CA G:HIS109 4.5 84.2 1.0
CB G:LYS88 4.5 79.9 1.0
C G:HIS87 4.6 82.2 1.0
CG G:LYS88 4.6 83.6 1.0
CG G:TYR108 4.6 86.4 1.0
CD1 G:TRP111 4.8 76.1 1.0
C G:TYR108 4.9 77.4 1.0
NE1 G:TRP111 4.9 78.4 1.0
CA G:LYS88 5.0 79.3 1.0

Iron binding site 8 out of 9 in 8h2t

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Iron binding site 8 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe501

b:123.0
occ:1.00
FE2 G:FES501 0.0 123.0 1.0
S1 G:FES501 2.2 101.7 1.0
S2 G:FES501 2.2 106.2 1.0
SG G:CYS106 2.3 85.4 1.0
SG G:CYS85 2.3 79.9 1.0
FE1 G:FES501 2.7 110.5 1.0
CB G:CYS85 3.1 69.4 1.0
CB G:CYS106 3.2 78.1 1.0
CB G:HIS87 3.7 84.3 1.0
CB G:TYR108 4.4 75.5 1.0
ND1 G:HIS87 4.5 79.1 1.0
CA G:CYS85 4.5 77.6 1.0
N G:HIS87 4.5 83.2 1.0
N G:LYS88 4.6 75.7 1.0
CG G:HIS87 4.6 84.9 1.0
ND1 G:HIS109 4.6 78.6 1.0
CB G:SER90 4.6 82.8 1.0
CA G:CYS106 4.6 79.6 1.0
CB G:TRP111 4.7 74.6 1.0
N G:HIS109 4.7 82.1 1.0
CA G:HIS87 4.7 78.2 1.0
CG G:TRP111 4.9 75.2 1.0
N G:SER90 4.9 78.2 1.0
C G:CYS85 4.9 81.9 1.0
O G:SER90 5.0 93.9 1.0

Iron binding site 9 out of 9 in 8h2t

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Iron binding site 9 out of 9 in the Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of Iadd/E Dioxygenase Bound with Iaa within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe503

b:144.6
occ:1.00
OD2 G:ASP377 2.0 98.6 1.0
OD1 G:ASP377 2.1 101.4 1.0
NE2 G:HIS216 2.2 79.2 1.0
OD1 G:ASN210 2.3 96.9 1.0
CG G:ASP377 2.3 95.3 1.0
NE2 G:HIS221 2.7 90.0 1.0
CE1 G:HIS216 2.9 84.4 1.0
ND2 G:ASN210 2.9 97.1 1.0
CG G:ASN210 2.9 94.1 1.0
CD2 G:HIS216 3.0 77.1 1.0
CE1 G:HIS221 3.4 95.5 1.0
CB G:ASP377 3.8 86.0 1.0
ND1 G:HIS216 3.8 84.3 1.0
CD2 G:HIS221 3.9 90.8 1.0
CG G:HIS216 3.9 80.8 1.0
CB G:ASN210 4.4 90.7 1.0
ND1 G:HIS221 4.6 90.2 1.0
O G:ASN210 4.7 101.3 1.0
CA G:ASP377 4.7 87.8 1.0
OH G:TYR381 4.7 92.5 1.0
C8 G:IAC502 4.8 110.8 1.0
N G:IAC502 4.9 109.9 1.0
CG G:HIS221 4.9 87.2 1.0

Reference:

Y.Ma, Z.Li, G.Yu, H.Zhang. Cryo-Em Structure of A Bacterial Dioxygenase To Be Published.
Page generated: Sat Aug 10 05:06:44 2024

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