2OFX
crystal structure of the APSK domain of human PAPSS1 in complex with ADPMg and PAPS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | THR66 |
| A | PPS1100 |
| A | ADP1300 |
| A | HOH1327 |
| A | HOH1358 |
| A | HOH1363 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ADP1400 |
| B | HOH1410 |
| B | HOH1438 |
| B | HOH1460 |
| B | THR66 |
| B | ASP87 |
| B | PPS1200 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | ARG139 |
| A | ASN140 |
| A | GLU155 |
| A | PRO195 |
| A | GLU196 |
| A | ALA197 |
| A | PRO198 |
| A | HOH1365 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| B | ARG139 |
| B | ASN140 |
| B | GLU155 |
| B | PRO195 |
| B | GLU196 |
| B | ALA197 |
| B | PRO198 |
| B | HOH1449 |
| B | HOH1497 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 403 |
| Chain | Residue |
| A | PRO161 |
| A | HIS163 |
| B | TYR75 |
| B | HIS79 |
| B | GLN214 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 404 |
| Chain | Residue |
| A | TYR75 |
| A | HIS79 |
| A | GLN214 |
| B | PRO161 |
| B | HIS163 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE PPS A 1100 |
| Chain | Residue |
| A | SER61 |
| A | LYS65 |
| A | GLY88 |
| A | ASP89 |
| A | ARG92 |
| A | PHE101 |
| A | ARG106 |
| A | ASN109 |
| A | PHE131 |
| A | ILE132 |
| A | SER133 |
| A | PRO134 |
| A | LYS171 |
| A | LEU173 |
| A | LYS183 |
| A | GLY184 |
| A | PHE185 |
| A | THR186 |
| A | MG301 |
| A | ADP1300 |
| A | HOH1327 |
| A | HOH1329 |
| A | HOH1339 |
| A | HOH1358 |
| A | HOH1363 |
| B | THR26 |
| B | ASN27 |
| B | VAL28 |
| B | HOH1407 |
| B | HOH1452 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE PPS B 1200 |
| Chain | Residue |
| B | HOH1460 |
| A | THR26 |
| A | ASN27 |
| A | VAL28 |
| A | HOH1351 |
| B | SER61 |
| B | LYS65 |
| B | GLY88 |
| B | ASP89 |
| B | ARG92 |
| B | PHE101 |
| B | ARG106 |
| B | ASN109 |
| B | PHE131 |
| B | ILE132 |
| B | SER133 |
| B | PRO134 |
| B | LYS171 |
| B | LEU173 |
| B | LYS183 |
| B | GLY184 |
| B | PHE185 |
| B | THR186 |
| B | MG302 |
| B | ADP1400 |
| B | HOH1417 |
| B | HOH1432 |
| B | HOH1438 |
| B | HOH1458 |
| B | HOH1459 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 1300 |
| Chain | Residue |
| A | LEU60 |
| A | GLY62 |
| A | ALA63 |
| A | GLY64 |
| A | LYS65 |
| A | THR66 |
| A | THR67 |
| A | VAL68 |
| A | ARG168 |
| A | VAL170 |
| A | THR204 |
| A | CYS207 |
| A | ASP208 |
| A | VAL209 |
| A | CYS212 |
| A | MG301 |
| A | PPS1100 |
| A | HOH1327 |
| A | HOH1343 |
| A | HOH1358 |
| A | HOH1373 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP B 1400 |
| Chain | Residue |
| B | LEU60 |
| B | SER61 |
| B | GLY62 |
| B | ALA63 |
| B | GLY64 |
| B | LYS65 |
| B | THR66 |
| B | THR67 |
| B | VAL68 |
| B | ARG168 |
| B | VAL170 |
| B | THR204 |
| B | CYS207 |
| B | ASP208 |
| B | VAL209 |
| B | CYS212 |
| B | MG302 |
| B | PPS1200 |
| B | HOH1410 |
| B | HOH1438 |
| B | HOH1457 |
| B | HOH1458 |
| B | HOH1478 |
| B | HOH1495 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15755455, ECO:0000269|PubMed:17276460, ECO:0000269|PubMed:17540769, ECO:0007744|PDB:1X6V, ECO:0007744|PDB:1XJQ, ECO:0007744|PDB:1XNJ, ECO:0007744|PDB:2OFX, ECO:0007744|PDB:2PEY, ECO:0007744|PDB:2PEZ |
| Chain | Residue | Details |
| A | GLY62 | |
| B | GLY62 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17276460, ECO:0007744|PDB:2OFX |
| Chain | Residue | Details |
| A | ASP89 | |
| A | PHE101 | |
| A | LYS171 | |
| B | ASP89 | |
| B | PHE101 | |
| B | LYS171 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17276460, ECO:0000305|PubMed:17540769, ECO:0007744|PDB:2OFX, ECO:0007744|PDB:2PEZ |
| Chain | Residue | Details |
| A | ARG106 | |
| A | ILE132 | |
| A | GLY184 | |
| B | ARG106 | |
| B | ILE132 | |
| B | GLY184 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15755455, ECO:0000269|PubMed:17276460, ECO:0000269|PubMed:17540769, ECO:0007744|PDB:1X6V, ECO:0007744|PDB:1XJQ, ECO:0007744|PDB:1XNJ, ECO:0007744|PDB:2OFW, ECO:0007744|PDB:2OFX, ECO:0007744|PDB:2PEY, ECO:0007744|PDB:2PEZ |
| Chain | Residue | Details |
| A | CYS207 | |
| B | CYS207 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17276460, ECO:0007744|PDB:2OFX |
| Chain | Residue | Details |
| A | CYS212 | |
| B | CYS212 |
