2H31
Crystal structure of human PAICS, a bifunctional carboxylase and synthetase in purine biosynthesis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| A | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009113 | biological_process | purine nucleobase biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043727 | molecular_function | 5-amino-4-imidazole carboxylate lyase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CO2 A 426 |
| Chain | Residue |
| A | HIS303 |
| A | HIS303 |
| A | SER332 |
| A | SER332 |
| A | ASN333 |
| A | ASN333 |
| A | GLY334 |
| A | GLY334 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17224163, ECO:0007744|PDB:2H31 |
| Chain | Residue | Details |
| A | ASN333 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | THR3 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9DCL9 |
| Chain | Residue | Details |
| A | GLU23 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PRO28 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCL9 |
| Chain | Residue | Details |
| A | ASP37 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PHE108 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PRO239 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | ASN248 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR275 |
