2BCO
X-ray structure of succinylglutamate desuccinalase from Vibrio Parahaemolyticus (RIMD 2210633) at the resolution 2.3 A, Northeast Structural Genomics Target Vpr14
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009017 | molecular_function | succinylglutamate desuccinylase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009017 | molecular_function | succinylglutamate desuccinylase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS63 |
| A | GLU66 |
| A | HIS155 |
| A | HOH584 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | HIS63 |
| B | GLU66 |
| B | HIS155 |
| B | HOH551 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00767","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
