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Iron in PDB 2g36: Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution

Enzymatic activity of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution

All present enzymatic activity of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution, PDB code: 2g36 was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.64 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 122.890, 152.730, 53.070, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 25.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution (pdb code 2g36). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution, PDB code: 2g36:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 2g36

Go back to Iron Binding Sites List in 2g36
Iron binding site 1 out of 4 in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:28.6
occ:1.00
 FE1 A:SF4400 0.0 28.6 1.0
S4 A:SF4400 2.3 28.7 1.0
S2 A:SF4400 2.3 36.1 1.0
S3 A:SF4400 2.3 30.9 1.0
SG A:CYS259 2.3 32.6 1.0
FE4 A:SF4400 2.6 26.8 1.0
FE2 A:SF4400 2.7 27.4 1.0
FE3 A:SF4400 2.7 24.4 1.0
CB A:CYS259 3.2 29.9 1.0
S1 A:SF4400 3.9 26.7 1.0
CA A:CYS259 4.3 29.6 1.0
NH1 A:ARG224 4.3 16.5 1.0
CD A:ARG224 4.3 25.4 1.0
CG A:PRO233 4.6 27.7 1.0
SG A:CYS236 4.7 30.9 1.0
SG A:CYS266 4.7 25.6 1.0
SG A:CYS269 4.8 30.6 1.0
CA A:PRO233 4.9 28.1 1.0
N A:PRO233 5.0 27.6 1.0
CB A:PRO233 5.0 28.5 1.0

Iron binding site 2 out of 4 in 2g36

Go back to Iron Binding Sites List in 2g36
Iron binding site 2 out of 4 in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:27.4
occ:1.00
 FE2 A:SF4400 0.0 27.4 1.0
SG A:CYS236 2.3 30.9 1.0
S1 A:SF4400 2.3 26.7 1.0
S3 A:SF4400 2.3 30.9 1.0
S4 A:SF4400 2.3 28.7 1.0
FE4 A:SF4400 2.6 26.8 1.0
FE3 A:SF4400 2.7 24.4 1.0
FE1 A:SF4400 2.7 28.6 1.0
CB A:CYS236 3.4 29.1 1.0
S2 A:SF4400 3.9 36.1 1.0
CB A:VAL238 4.1 24.8 1.0
CB A:THR220 4.1 29.4 1.0
CG2 A:THR220 4.3 29.5 1.0
N A:ASP221 4.4 32.8 1.0
CA A:THR220 4.5 31.1 1.0
CG2 A:VAL238 4.5 19.9 1.0
SG A:CYS266 4.7 25.6 1.0
CA A:CYS236 4.7 28.2 1.0
N A:TRP239 4.8 27.2 1.0
SG A:CYS269 4.8 30.6 1.0
CG1 A:VAL238 4.8 18.9 1.0
SG A:CYS259 4.9 32.6 1.0
C A:THR220 5.0 32.9 1.0

Iron binding site 3 out of 4 in 2g36

Go back to Iron Binding Sites List in 2g36
Iron binding site 3 out of 4 in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:24.4
occ:1.00
 FE3 A:SF4400 0.0 24.4 1.0
SG A:CYS269 2.3 30.6 1.0
S2 A:SF4400 2.3 36.1 1.0
S1 A:SF4400 2.3 26.7 1.0
S4 A:SF4400 2.3 28.7 1.0
FE2 A:SF4400 2.7 27.4 1.0
FE1 A:SF4400 2.7 28.6 1.0
FE4 A:SF4400 2.7 26.8 1.0
CB A:CYS269 3.2 28.1 1.0
S3 A:SF4400 4.0 30.9 1.0
CG1 A:VAL255 4.4 25.1 1.0
CG1 A:VAL238 4.5 18.9 1.0
CA A:CYS269 4.6 27.3 1.0
CB A:VAL238 4.7 24.8 1.0
SG A:CYS266 4.7 25.6 1.0
CA A:CYS266 4.7 23.6 1.0
SG A:CYS236 4.8 30.9 1.0
SG A:CYS259 4.8 32.6 1.0
CB A:CYS259 4.9 29.9 1.0

Iron binding site 4 out of 4 in 2g36

Go back to Iron Binding Sites List in 2g36
Iron binding site 4 out of 4 in the Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Tryptophanyl-Trna Synthetase (Ec 6.1.1.2) (Tryptophan-Trna Ligase)(Trprs) (TM0492) From Thermotoga Maritima at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:26.8
occ:1.00
 FE4 A:SF4400 0.0 26.8 1.0
SG A:CYS266 2.3 25.6 1.0
S3 A:SF4400 2.3 30.9 1.0
S1 A:SF4400 2.3 26.7 1.0
S2 A:SF4400 2.3 36.1 1.0
FE2 A:SF4400 2.6 27.4 1.0
FE1 A:SF4400 2.6 28.6 1.0
FE3 A:SF4400 2.7 24.4 1.0
CB A:CYS266 3.3 22.2 1.0
CA A:CYS266 3.7 23.6 1.0
S4 A:SF4400 3.9 28.7 1.0
NH1 A:ARG224 4.0 16.5 1.0
CD A:ARG224 4.1 25.4 1.0
CG2 A:THR220 4.2 29.5 1.0
CB A:THR220 4.2 29.4 1.0
N A:CYS266 4.3 23.9 1.0
SG A:CYS259 4.7 32.6 1.0
SG A:CYS269 4.7 30.6 1.0
SG A:CYS236 4.7 30.9 1.0
CB A:CYS269 4.7 28.1 1.0
CZ A:ARG224 4.9 23.0 1.0
NE A:ARG224 4.9 19.9 1.0
C A:CYS266 5.0 25.3 1.0
OG1 A:THR220 5.0 26.7 1.0

Reference:

G.W.Han, X.L.Yang, D.Mcmullan, Y.E.Chong, S.S.Krishna, C.L.Rife, D.Weekes, S.M.Brittain, P.Abdubek, E.Ambing, T.Astakhova, H.L.Axelrod, D.Carlton, J.Caruthers, H.J.Chiu, T.Clayton, L.Duan, J.Feuerhelm, J.C.Grant, S.K.Grzechnik, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, A.Kumar, D.Marciano, M.D.Miller, A.T.Morse, E.Nigoghossian, L.Okach, J.Paulsen, R.Reyes, H.Van Den Bedem, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, M.A.Elsliger, P.Schimmel, I.A.Wilson. Structure of A Tryptophanyl-Trna Synthetase Containing An Iron-Sulfur Cluster. Acta Crystallogr.,Sect.F V. 66 1326 2010.
ISSN: ESSN 1744-3091
PubMed: 20944229
DOI: 10.1107/S1744309110037619
Page generated: Thu Jul 17 01:26:03 2025

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