6JUY
Crystal Structure of ArgZ, apo structure, an Arginine Dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:31914412 |
| Chain | Residue | Details |
| A | HIS168 | |
| B | HIS168 | |
| C | HIS168 | |
| D | HIS168 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:31914412 |
| Chain | Residue | Details |
| A | CYS264 | |
| B | CYS264 | |
| C | CYS264 | |
| D | CYS264 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31914412, ECO:0007744|PDB:6JV0 |
| Chain | Residue | Details |
| A | ASN22 | |
| B | ARG90 | |
| B | ARG139 | |
| B | HIS168 | |
| B | ALA258 | |
| B | CYS264 | |
| C | ASN22 | |
| C | ASN71 | |
| C | ARG90 | |
| C | ARG139 | |
| C | HIS168 | |
| A | ASN71 | |
| C | ALA258 | |
| C | CYS264 | |
| D | ASN22 | |
| D | ASN71 | |
| D | ARG90 | |
| D | ARG139 | |
| D | HIS168 | |
| D | ALA258 | |
| D | CYS264 | |
| A | ARG90 | |
| A | ARG139 | |
| A | HIS168 | |
| A | ALA258 | |
| A | CYS264 | |
| B | ASN22 | |
| B | ASN71 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31914412, ECO:0007744|PDB:6JUZ, ECO:0007744|PDB:6JV1 |
| Chain | Residue | Details |
| A | ASP170 | |
| B | ASP170 | |
| C | ASP170 | |
| D | ASP170 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8YMD9 |
| Chain | Residue | Details |
| A | ASN525 | |
| A | VAL681 | |
| B | ASN525 | |
| B | ALA526 | |
| B | ASP604 | |
| B | SER636 | |
| B | MET637 | |
| B | LEU638 | |
| B | HIS639 | |
| B | ASP657 | |
| B | ASP680 | |
| A | ALA526 | |
| B | VAL681 | |
| C | ASN525 | |
| C | ALA526 | |
| C | ASP604 | |
| C | SER636 | |
| C | MET637 | |
| C | LEU638 | |
| C | HIS639 | |
| C | ASP657 | |
| C | ASP680 | |
| A | ASP604 | |
| C | VAL681 | |
| D | ASN525 | |
| D | ALA526 | |
| D | ASP604 | |
| D | SER636 | |
| D | MET637 | |
| D | LEU638 | |
| D | HIS639 | |
| D | ASP657 | |
| D | ASP680 | |
| A | SER636 | |
| D | VAL681 | |
| A | MET637 | |
| A | LEU638 | |
| A | HIS639 | |
| A | ASP657 | |
| A | ASP680 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Key determinant for dihydrolase activity => ECO:0000305|PubMed:31914412 |
| Chain | Residue | Details |
| A | ASN71 | |
| B | ASN71 | |
| C | ASN71 | |
| D | ASN71 |
