4PQA
Crystal Structure of succinyl-diaminopimelate desuccinylase from Neisseria meningitidis MC58 in complex with the Inhibitor Captopril
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008777 | molecular_function | acetylornithine deacetylase activity |
| A | 0009014 | molecular_function | succinyl-diaminopimelate desuccinylase activity |
| A | 0009085 | biological_process | L-lysine biosynthetic process |
| A | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE X8Z A 401 |
| Chain | Residue |
| A | ASP101 |
| A | ASN346 |
| A | ILE349 |
| A | ZN403 |
| A | ZN404 |
| A | HOH532 |
| A | HOH840 |
| A | GLU135 |
| A | GLU136 |
| A | GLU164 |
| A | ARG179 |
| A | HIS195 |
| A | TYR198 |
| A | GLY325 |
| A | THR326 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | HIS195 |
| A | ASN246 |
| A | ARG259 |
| A | GLY325 |
| A | THR326 |
| A | HOH760 |
| A | HOH789 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HIS68 |
| A | ASP101 |
| A | GLU164 |
| A | X8Z401 |
| A | ZN404 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 404 |
| Chain | Residue |
| A | ASP101 |
| A | GLU136 |
| A | HIS350 |
| A | X8Z401 |
| A | ZN403 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P44514","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P44514","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26186504","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33721990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4O23","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PQA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5UEJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"source":"PubMed","id":"33721990","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"A0A1S8KJG1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
