3IT4
The Crystal Structure of Ornithine Acetyltransferase from Mycobacterium tuberculosis (Rv1653) at 1.7 A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
A | 0006526 | biological_process | L-arginine biosynthetic process |
B | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
B | 0006526 | biological_process | L-arginine biosynthetic process |
C | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
C | 0006526 | biological_process | L-arginine biosynthetic process |
D | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
D | 0006526 | biological_process | L-arginine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 500 |
Chain | Residue |
A | ALA52 |
A | GLY53 |
A | LEU72 |
A | THR73 |
A | HOH233 |
A | HOH237 |
A | HOH354 |
B | GLU217 |
B | ARG221 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 501 |
Chain | Residue |
B | HOH174 |
B | HOH191 |
B | ASP234 |
B | GLY235 |
B | ARG308 |
B | HOH439 |
D | ARG308 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT B 601 |
Chain | Residue |
B | HOH193 |
B | ASN322 |
B | ARG325 |
B | HOH425 |
B | HOH564 |
C | LEU129 |
C | MET193 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 502 |
Chain | Residue |
C | ASP158 |
C | HIS162 |
C | HOH246 |
C | HOH393 |
C | HOH466 |
D | HOH130 |
D | GLN257 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BEZ C 503 |
Chain | Residue |
C | ARG9 |
C | GLN14 |
C | HIS177 |
D | ARG221 |
D | ARG222 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT D 601 |
Chain | Residue |
D | ASN322 |
D | ARG325 |
D | HOH432 |
D | HOH590 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
B | THR200 | |
D | THR200 | |
C | THR166 | |
C | LYS189 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | THR200 | |
B | GLU280 | |
B | ASN399 | |
B | SER404 | |
D | THR200 | |
D | GLU280 | |
D | ASN399 | |
D | SER404 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by autolysis |
Chain | Residue | Details |
A | ALA199 | |
C | ALA199 |