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1VK3

Crystal structure of Phosphoribosylformylglycinamidine synthase II (TM1246) from Thermotoga maritima at 2.15 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004642molecular_functionphosphoribosylformylglycinamidine synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS01023
Number of Residues13
DetailsPTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI
ChainResidueDetails
ATHR246-ILE258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
ChainResidueDetails
AHIS32

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17154526
ChainResidueDetails
AHIS72

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
ChainResidueDetails
ATYR35
ALYS68
AASN442

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
ChainResidueDetails
AGLU70
AASP94
AASP236
AASN478

site_idSWS_FT_FI5
Number of Residues7
DetailsBINDING:
ChainResidueDetails
ASER71
AARG93
AGLY136
AGLY189
AGLN208
AGLU280
ASER480

site_idSWS_FT_FI6
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:17154526
ChainResidueDetails
AASP107
AGLY388
ALYS429
ASER549
AHIS556

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
ChainResidueDetails
AGLY477

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PDB entries from 2024-07-24

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