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3VIU

Crystal structure of PurL from thermus thermophilus

Replaces:  3AC6
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 PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 800
ChainResidue
ATYR44
AASN523
AVAL524
AHOH781
APEG920
AGLY66
AGLU67
ALYS83
AGLU85
AASP109
AASP485
ASER521
AGLY522

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 900
ChainResidue
AHIS41
ASER86
AHIS87
AASN88
AHIS89
ASER525
AHOH789

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 910
ChainResidue
AASP430
AASN472
AASP620
AHOH952
AHOH1019
AHOH1020

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 920
ChainResidue
ATYR44
AARG48
AADP800
AHOH983
AHOH1017

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00420
ChainResidueDetails
AHIS41

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00420
ChainResidueDetails
AHIS87

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLY66
ALYS83
AASP109
AASP485
AGLY522

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ASER86
ASER525

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00420
ChainResidueDetails
AARG108
AGLY211
AGLN231
AGLU303

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22232163
ChainResidueDetails
AASP430
AASN472
AASP620

224201

PDB entries from 2024-08-28

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