1XNJ
APS complex of human PAPS synthetase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0001501 | biological_process | skeletal system development |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0034030 | biological_process | ribonucleoside bisphosphate biosynthetic process |
| A | 0034033 | biological_process | purine nucleoside bisphosphate biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050428 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0001501 | biological_process | skeletal system development |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0034030 | biological_process | ribonucleoside bisphosphate biosynthetic process |
| B | 0034033 | biological_process | purine nucleoside bisphosphate biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050428 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADX A 2900 |
| Chain | Residue |
| A | PHE418 |
| A | ARG522 |
| A | PRO524 |
| A | ALA525 |
| A | ARG561 |
| A | VAL562 |
| A | ALA563 |
| A | HOH2907 |
| A | HOH3123 |
| A | HOH3169 |
| A | HOH3173 |
| A | GLN419 |
| A | LEU420 |
| A | ARG421 |
| A | ASN422 |
| A | HIS428 |
| A | MET495 |
| A | VAL520 |
| A | GLY521 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 2800 |
| Chain | Residue |
| B | LEU60 |
| B | GLY62 |
| B | ALA63 |
| B | GLY64 |
| B | LYS65 |
| B | THR66 |
| B | THR67 |
| B | ARG168 |
| B | THR204 |
| B | CYS207 |
| B | ASP208 |
| B | VAL209 |
| B | CYS212 |
| B | HOH2963 |
| B | HOH2989 |
| B | HOH3006 |
| B | HOH3076 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADX B 2805 |
| Chain | Residue |
| B | SER61 |
| B | ARG92 |
| B | PHE101 |
| B | ARG106 |
| B | ASN109 |
| B | PHE131 |
| B | ILE132 |
| B | SER133 |
| B | PRO134 |
| B | LYS171 |
| B | LEU173 |
| B | LYS183 |
| B | PHE185 |
| B | THR186 |
| B | HOH3114 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADX B 2700 |
| Chain | Residue |
| B | PHE418 |
| B | GLN419 |
| B | LEU420 |
| B | ARG421 |
| B | ASN422 |
| B | HIS425 |
| B | HIS428 |
| B | LEU431 |
| B | MET495 |
| B | VAL520 |
| B | GLY521 |
| B | ARG522 |
| B | PRO524 |
| B | ALA525 |
| B | ARG561 |
| B | VAL562 |
| B | ALA563 |
| B | HOH3020 |
| B | HOH3059 |
| B | HOH3063 |
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 |
| B | GLY62 | |
| A | GLY62 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17276460, ECO:0007744|PDB:2OFX |
| Chain | Residue | Details |
| B | ASP89 | |
| B | PHE101 | |
| B | LYS171 | |
| A | ASP89 | |
| A | PHE101 | |
| A | 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 |
| B | ARG106 | |
| B | ILE132 | |
| B | GLY184 | |
| A | ARG106 | |
| A | ILE132 | |
| A | 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 |
| B | CYS207 | |
| A | CYS207 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17276460, ECO:0007744|PDB:2OFX |
| Chain | Residue | Details |
| B | CYS212 | |
| A | CYS212 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15755455, ECO:0007744|PDB:1XJQ, ECO:0007744|PDB:1XNJ, ECO:0007744|PDB:2QJF |
| Chain | Residue | Details |
| B | GLN419 | |
| B | GLY521 | |
| B | ALA563 | |
| A | GLN419 | |
| A | GLY521 | |
| A | ALA563 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| B | MET1 | |
| A | MET1 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q60967 |
| Chain | Residue | Details |
| B | LYS12 | |
| A | LYS12 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | HIS428 | |
| B | ARG421 | |
| B | HIS425 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | HIS428 | |
| A | ARG421 | |
| A | HIS425 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | ARG522 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | ARG522 |
