4RZB
The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-formimino-L-Aspartate, SOAKED WITH MERCURY
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 |
| B | 0005829 | cellular_component | cytosol |
| B | 0006547 | biological_process | L-histidine metabolic process |
| B | 0006548 | biological_process | L-histidine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0019239 | molecular_function | deaminase activity |
| B | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| B | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050416 | molecular_function | formimidoylglutamate deiminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NFQ A 501 |
| Chain | Residue |
| A | HIS58 |
| A | HOH620 |
| A | HOH652 |
| A | HOH677 |
| A | HOH678 |
| A | HOH1040 |
| A | GLN61 |
| A | PHE78 |
| A | ARG82 |
| A | TYR121 |
| A | HIS206 |
| A | ARG209 |
| A | GLU235 |
| A | LEU298 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | HIS56 |
| A | HIS58 |
| A | HIS232 |
| A | ASP320 |
| A | HOH1040 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 503 |
| Chain | Residue |
| A | PHE164 |
| A | CYS243 |
| A | SER247 |
| A | HOH1083 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG A 504 |
| Chain | Residue |
| A | GLU98 |
| A | CYS102 |
| A | HG505 |
| A | HOH739 |
| A | HOH758 |
| A | HOH1057 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 505 |
| Chain | Residue |
| A | CYS102 |
| A | HG504 |
| A | HOH758 |
| A | HOH812 |
| A | HOH934 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | GLY179 |
| A | SER180 |
| A | GLN215 |
| A | HOH668 |
| A | HOH915 |
| A | HOH1051 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | SER2 |
| A | ILE23 |
| A | SER24 |
| A | GLY425 |
| A | HOH836 |
| A | HOH908 |
| A | HOH929 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NFQ B 501 |
| Chain | Residue |
| B | HIS58 |
| B | GLN61 |
| B | PHE78 |
| B | ARG82 |
| B | TYR121 |
| B | HIS206 |
| B | ARG209 |
| B | GLU235 |
| B | LEU298 |
| B | ASP320 |
| B | HOH601 |
| B | HOH620 |
| B | HOH638 |
| B | HOH674 |
| B | HOH677 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | HIS56 |
| B | HIS58 |
| B | HIS232 |
| B | ASP320 |
| B | HOH601 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 503 |
| Chain | Residue |
| B | PHE164 |
| B | CYS243 |
| B | SER247 |
| B | HOH1014 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 504 |
| Chain | Residue |
| B | CYS102 |
| B | HG505 |
| B | HOH903 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 505 |
| Chain | Residue |
| B | GLU98 |
| B | CYS102 |
| B | HG504 |
| B | HOH726 |
| B | HOH797 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 506 |
| Chain | Residue |
| A | ILE302 |
| B | ILE302 |
| B | HOH828 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| Chain | Residue |
| B | GLY179 |
| B | SER180 |
| B | GLU181 |
| B | GLN215 |
| B | HOH695 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 508 |
| Chain | Residue |
| B | GLN237 |
| B | ARG250 |
| B | HIS272 |
| B | HOH1011 |
| B | HOH1012 |
| B | HOH1013 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 8 |
| 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 | 12 |
| 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 |
