4RZI
Crystal structure of PhaB from Synechocystis sp. PCC 6803
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| C | 0030497 | biological_process | fatty acid elongation |
| C | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SisgergnvgQtnYSATKAGViGMMkSLA |
| Chain | Residue | Details |
| B | SER134-ALA162 |
| site_id | PS01108 |
| Number of Residues | 19 |
| Details | RIBOSOMAL_L24 Ribosomal protein L24 signature. EDkViVVtGgnRGigaAiV |
| Chain | Residue | Details |
| B | GLU7-VAL25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001, ECO:0000305|PubMed:26358291 |
| Chain | Residue | Details |
| B | TYR147 | |
| A | TYR147 | |
| C | TYR147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14697 |
| Chain | Residue | Details |
| B | ARG18 | |
| A | GLY178 | |
| C | ARG18 | |
| C | ASN82 | |
| C | ASN141 | |
| C | PRO177 | |
| C | GLY178 | |
| B | ASN82 | |
| B | ASN141 | |
| B | PRO177 | |
| B | GLY178 | |
| A | ARG18 | |
| A | ASN82 | |
| A | ASN141 | |
| A | PRO177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:26358291 |
| Chain | Residue | Details |
| B | SER134 | |
| A | SER134 | |
| C | SER134 |
