1YNI
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 | arginine catabolic process |
| A | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019544 | biological_process | arginine catabolic process to glutamate |
| A | 0019545 | biological_process | arginine catabolic process to succinate |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | arginine catabolic process |
| B | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019544 | biological_process | arginine catabolic process to glutamate |
| B | 0019545 | biological_process | arginine catabolic process to succinate |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0006527 | biological_process | arginine catabolic process |
| C | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019544 | biological_process | arginine catabolic process to glutamate |
| C | 0019545 | biological_process | arginine catabolic process to succinate |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0006525 | biological_process | arginine metabolic process |
| D | 0006527 | biological_process | arginine catabolic process |
| D | 0009015 | molecular_function | N-succinylarginine dihydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019544 | biological_process | arginine catabolic process to glutamate |
| D | 0019545 | biological_process | arginine catabolic process to succinate |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 2001 |
| Chain | Residue |
| A | LEU338 |
| A | LEU339 |
| A | ALA341 |
| A | ASN343 |
| A | ILE345 |
| A | HOH2155 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 2002 |
| Chain | Residue |
| B | ASN343 |
| B | ILE345 |
| B | HOH2101 |
| B | LEU338 |
| B | LEU339 |
| B | ALA341 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 2003 |
| Chain | Residue |
| C | LEU338 |
| C | LEU339 |
| C | ALA341 |
| C | ASN343 |
| C | ILE345 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 2004 |
| Chain | Residue |
| D | LEU338 |
| D | LEU339 |
| D | ALA341 |
| D | ASN343 |
| D | ILE345 |
| D | HOH2163 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SUG A 1001 |
| Chain | Residue |
| A | HIS17 |
| A | ALA19 |
| A | GLY20 |
| A | LEU21 |
| A | SER22 |
| A | ASN25 |
| A | SER28 |
| A | TRP107 |
| A | ALA109 |
| A | ASN110 |
| A | HIS137 |
| A | ARG138 |
| A | ALA177 |
| A | ARG212 |
| A | PHE247 |
| A | HIS248 |
| A | ASP250 |
| A | ASN359 |
| A | GLY360 |
| A | SER365 |
| A | HOH2128 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SUG B 1002 |
| Chain | Residue |
| B | HIS17 |
| B | ALA19 |
| B | GLY20 |
| B | LEU21 |
| B | SER22 |
| B | ASN25 |
| B | SER28 |
| B | TRP107 |
| B | ALA109 |
| B | ASN110 |
| B | HIS137 |
| B | ARG138 |
| B | ALA177 |
| B | ARG212 |
| B | PHE247 |
| B | HIS248 |
| B | ASP250 |
| B | ASN359 |
| B | GLY360 |
| B | SER365 |
| B | HOH2009 |
| B | HOH2134 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SUG C 1003 |
| Chain | Residue |
| C | HIS17 |
| C | ALA19 |
| C | GLY20 |
| C | LEU21 |
| C | SER22 |
| C | ASN25 |
| C | SER28 |
| C | TRP107 |
| C | ALA109 |
| C | ASN110 |
| C | HIS137 |
| C | ARG138 |
| C | ALA177 |
| C | ARG212 |
| C | PHE247 |
| C | HIS248 |
| C | ASP250 |
| C | ASN306 |
| C | ASN359 |
| C | GLY360 |
| C | SER365 |
| C | HOH2056 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SUG D 1004 |
| Chain | Residue |
| D | ARG138 |
| D | ALA177 |
| D | ARG212 |
| D | PHE247 |
| D | HIS248 |
| D | ASP250 |
| D | ASN359 |
| D | GLY360 |
| D | SER365 |
| D | HOH2075 |
| D | HIS17 |
| D | ALA19 |
| D | GLY20 |
| D | LEU21 |
| D | SER22 |
| D | ASN25 |
| D | SER28 |
| D | TRP107 |
| D | ALA109 |
| D | ASN110 |
| D | HIS137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU174 | |
| A | HIS248 | |
| B | GLU174 | |
| B | HIS248 | |
| C | GLU174 | |
| C | HIS248 | |
| D | GLU174 | |
| D | HIS248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | SER365 | |
| B | SER365 | |
| C | SER365 | |
| D | SER365 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA19 | |
| B | ARG212 | |
| B | ASP250 | |
| B | ASN359 | |
| C | ALA19 | |
| C | ASN110 | |
| C | HIS137 | |
| C | ARG212 | |
| C | ASP250 | |
| C | ASN359 | |
| D | ALA19 | |
| A | ASN110 | |
| D | ASN110 | |
| D | HIS137 | |
| D | ARG212 | |
| D | ASP250 | |
| D | ASN359 | |
| A | HIS137 | |
| A | ARG212 | |
| A | ASP250 | |
| A | ASN359 | |
| B | ALA19 | |
| B | ASN110 | |
| B | HIS137 |
