3IC1
Crystal structure of zinc-bound succinyl-diaminopimelate desuccinylase from Haemophilus influenzae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009014 | molecular_function | succinyl-diaminopimelate desuccinylase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009014 | molecular_function | succinyl-diaminopimelate desuccinylase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | HIS67 |
| A | ASP100 |
| A | GLU134 |
| A | GLU135 |
| A | GLU163 |
| A | HOH482 |
| A | ZN1002 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | HIS349 |
| A | HOH482 |
| A | ZN1001 |
| A | ASP100 |
| A | GLU135 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 3002 |
| Chain | Residue |
| A | LYS269 |
| A | TRP287 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 378 |
| Chain | Residue |
| A | ARG178 |
| A | ARG179 |
| A | ARG258 |
| A | GLY322 |
| A | GLY323 |
| A | GLY324 |
| A | HOH397 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 379 |
| Chain | Residue |
| A | GLY299 |
| A | LYS300 |
| A | HOH380 |
| B | GLU87 |
| B | HOH458 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 3001 |
| Chain | Residue |
| B | LEU344 |
| B | SER356 |
| B | ASP359 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 378 |
| Chain | Residue |
| B | ARG258 |
| B | THR325 |
| B | ARG329 |
| B | HOH445 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 379 |
| Chain | Residue |
| B | GLY323 |
| B | GLY324 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 380 |
| Chain | Residue |
| B | ARG178 |
| B | ARG179 |
| B | ARG258 |
| B | GLY322 |
| B | HOH390 |
| B | HOH466 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1002 |
| Chain | Residue |
| B | ASP100 |
| B | GLU135 |
| B | HIS349 |
| B | HOH479 |
| B | ZN1001 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1001 |
| Chain | Residue |
| B | HIS67 |
| B | ASP100 |
| B | GLU134 |
| B | GLU163 |
| B | HOH479 |
| B | ZN1002 |
Functional Information from PROSITE/UniProt
| site_id | PS00758 |
| Number of Residues | 10 |
| Details | ARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. IAFAGHtDVV |
| Chain | Residue | Details |
| A | ILE62-VAL71 |
| site_id | PS00759 |
| Number of Residues | 40 |
| Details | ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. AADmKGslAamIvaaeeyvkanpnhkgt.IaLLItsDEEaT |
| Chain | Residue | Details |
| A | ALA98-THR137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"20138056","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20138056","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20138056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ISZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20138056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU134 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLU134 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU135 | |
| A | ASP100 | |
| A | HIS349 | |
| A | GLU134 | |
| A | HIS67 | |
| A | GLU163 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLU135 | |
| B | ASP100 | |
| B | HIS349 | |
| B | GLU134 | |
| B | HIS67 | |
| B | GLU163 |
