4RDW
The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-Glutaric acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006547 | biological_process | histidine metabolic process |
| A | 0006548 | biological_process | histidine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0019556 | biological_process | histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | histidine catabolic process to glutamate and formate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS56 |
| A | HIS58 |
| A | HIS232 |
| A | ASP320 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NGQ A 502 |
| Chain | Residue |
| A | TYR121 |
| A | HIS206 |
| A | ARG209 |
| A | GLU235 |
| A | LEU298 |
| A | HOH601 |
| A | HOH645 |
| A | HOH663 |
| A | HOH757 |
| A | HIS58 |
| A | GLN61 |
| A | PHE78 |
| A | ARG82 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ASP127 |
| A | ARG129 |
| A | GOL508 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | ALA222 |
| A | GLY223 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | TRP246 |
| A | SER247 |
| A | TRP254 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | LEU126 |
| A | ASP127 |
| A | GLN446 |
| A | GLU450 |
| A | HOH684 |
| A | HOH730 |
| A | HOH763 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | SER130 |
| A | TYR131 |
| A | ALA132 |
| A | GLU136 |
| A | ARG140 |
| A | ARG143 |
| A | HOH607 |
| A | HOH752 |
| A | HOH784 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 508 |
| Chain | Residue |
| A | GLU98 |
| A | ARG129 |
| A | ALA147 |
| A | EDO503 |
| A | HOH886 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A 509 |
| Chain | Residue |
| A | HIS124 |
| A | GLY128 |
| A | ARG129 |
| A | SER130 |
| A | ILE177 |
| A | HOH650 |
| A | HOH805 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17128965, ECO:0000305|PubMed:25559274 |
| Chain | Residue | Details |
| A | HIS269 | |
| A | ASP320 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25559274, ECO:0007744|PDB:3MDU, ECO:0007744|PDB:3MDW, ECO:0007744|PDB:4RDV, ECO:0007744|PDB:4RDW, ECO:0007744|PDB:4RZB |
| Chain | Residue | Details |
| A | HIS56 | |
| A | HIS58 | |
| A | HIS232 | |
| A | ASP320 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25559274, ECO:0007744|PDB:3MDU, ECO:0007744|PDB:3MDW, ECO:0007744|PDB:4RDV, ECO:0007744|PDB:4RDW, ECO:0007744|PDB:4RZB |
| Chain | Residue | Details |
| A | GLN61 | |
| A | ARG82 | |
| A | TYR121 | |
| A | HIS206 | |
| A | ARG209 | |
| A | GLU235 |
