2PEY
Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1
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 | 16 |
Details | BINDING SITE FOR RESIDUE ADX A 400 |
Chain | Residue |
A | ARG92 |
A | GLY184 |
A | PHE185 |
A | THR186 |
A | HOH414 |
A | HOH419 |
A | HOH444 |
A | HOH459 |
A | PHE101 |
A | ARG106 |
A | ASN109 |
A | PHE131 |
A | ILE132 |
A | SER133 |
A | PRO134 |
A | LEU173 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE DAT A 300 |
Chain | Residue |
A | LEU60 |
A | GLY62 |
A | ALA63 |
A | GLY64 |
A | LYS65 |
A | THR66 |
A | THR67 |
A | ARG168 |
A | THR204 |
A | CYS207 |
A | ASP208 |
A | VAL209 |
A | HOH414 |
A | HOH432 |
A | HOH443 |
A | HOH452 |
B | HIS163 |
B | GLN167 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE DAT B 227 |
Chain | Residue |
A | HIS163 |
A | GLN167 |
B | LEU60 |
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 | HOH251 |
B | HOH263 |
B | HOH277 |
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 |