1YNF
Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0006525 | biological_process | arginine metabolic process |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| E | 0006525 | biological_process | arginine metabolic process |
| E | 0006527 | biological_process | L-arginine catabolic process |
| E | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| E | 0042803 | molecular_function | protein homodimerization activity |
| F | 0006525 | biological_process | arginine metabolic process |
| F | 0006527 | biological_process | L-arginine catabolic process |
| F | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| F | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K E 448 |
| Chain | Residue |
| E | LEU338 |
| E | LEU339 |
| E | ALA341 |
| E | ASN343 |
| E | ILE345 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 448 |
| Chain | Residue |
| C | ILE345 |
| C | LEU338 |
| C | LEU339 |
| C | ALA341 |
| C | ASN343 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 448 |
| Chain | Residue |
| B | LEU338 |
| B | LEU339 |
| B | ALA341 |
| B | ASN343 |
| B | ILE345 |
| B | HOH620 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 448 |
| Chain | Residue |
| A | LEU338 |
| A | LEU339 |
| A | ALA341 |
| A | ASN343 |
| A | ILE345 |
| A | HOH620 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K F 448 |
| Chain | Residue |
| F | LEU338 |
| F | LEU339 |
| F | ALA341 |
| F | ASN343 |
| F | ILE345 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 448 |
| Chain | Residue |
| D | LEU338 |
| D | LEU339 |
| D | ALA341 |
| D | ASN343 |
| D | ILE345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {} |
| Chain | Residue | Details |
