1VK3
Crystal structure of Phosphoribosylformylglycinamidine synthase II (TM1246) from Thermotoga maritima at 2.15 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004642 | molecular_function | phosphoribosylformylglycinamidine synthase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS01023 |
Number of Residues | 13 |
Details | PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI |
Chain | Residue | Details |
A | THR246-ILE258 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 |
Chain | Residue | Details |
A | HIS32 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17154526 |
Chain | Residue | Details |
A | HIS72 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 |
Chain | Residue | Details |
A | TYR35 | |
A | LYS68 | |
A | ASN442 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 |
Chain | Residue | Details |
A | GLU70 | |
A | ASP94 | |
A | ASP236 | |
A | ASN478 |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | BINDING: |
Chain | Residue | Details |
A | SER71 | |
A | ARG93 | |
A | GLY136 | |
A | GLY189 | |
A | GLN208 | |
A | GLU280 | |
A | SER480 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17154526 |
Chain | Residue | Details |
A | ASP107 | |
A | GLY388 | |
A | LYS429 | |
A | SER549 | |
A | HIS556 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 |
Chain | Residue | Details |
A | GLY477 |