3MDU
The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-Glutamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006547 | biological_process | L-histidine metabolic process |
| A | 0006548 | biological_process | L-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 | L-histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | L-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 454 |
| Chain | Residue |
| A | HIS56 |
| A | HIS58 |
| A | HIS232 |
| A | ASP320 |
| A | HOH495 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NGQ A 455 |
| Chain | Residue |
| A | ARG82 |
| A | TYR121 |
| A | HIS206 |
| A | ARG209 |
| A | GLU235 |
| A | LEU298 |
| A | HOH495 |
| A | HOH499 |
| A | HOH514 |
| A | HOH562 |
| A | HIS58 |
| A | GLN61 |
| A | PHE78 |
| A | TRP81 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 456 |
| Chain | Residue |
| A | LEU126 |
| A | ASP127 |
| A | GLN446 |
| A | GLU450 |
| A | HOH575 |
| A | HOH595 |
| A | HOH632 |
| A | HOH753 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 457 |
| Chain | Residue |
| A | GLU98 |
| A | ARG129 |
| A | ALA147 |
| A | HOH573 |
| A | HOH740 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17128965","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3MDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
