4O23
Crystal structure of mono-zinc form of succinyl diaminopimelate desuccinylase from Neisseria meningitidis MC58
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 | 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 | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008777 | molecular_function | acetylornithine deacetylase activity |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS68 |
| A | ASP101 |
| A | GLU164 |
| A | HOH609 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS68 |
| B | ASP101 |
| B | GLU135 |
| B | GLU164 |
| B | HOH547 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | ASP101 |
| B | GLU136 |
| B | HIS350 |
| B | HOH547 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| A | HIS195 |
| A | ASN246 |
| B | ARG259 |
| B | GLY325 |
| B | THR326 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| A | ARG259 |
| A | HOH562 |
| B | HIS195 |
| B | ASN246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP70 | |
| B | ASP70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU135 | |
| B | GLU135 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS68 | |
| B | HIS350 | |
| A | ASP101 | |
| A | GLU136 | |
| A | GLU164 | |
| A | HIS350 | |
| B | HIS68 | |
| B | ASP101 | |
| B | GLU136 | |
| B | GLU164 |
