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4XTI

Structure of IMP dehydrogenase of Ashbya gossypii with IMP bound to the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue IMP A 601
ChainResidue
ASER74
AASP367
AGLY368
AGLY369
AMET388
AGLY390
AGLY391
ATYR414
AGLY416
AMET417
AGLY418
AMET76
AGLN448
AGLY449
AHOH703
AHOH785
AHOH817
AASN306
AARG325
AGLY331
ASER332
AILE333
ACYS334
ATHR336

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 602
ChainResidue
AGLY329
AGLY331
ACYS334
AGLU507
AGLY508
AGLY509

site_idAC3
Number of Residues22
Detailsbinding site for residue IMP B 601
ChainResidue
BSER74
BARG325
BGLY331
BSER332
BILE333
BCYS334
BTHR336
BASP367
BGLY368
BGLY369
BMET388
BGLY390
BGLY391
BTYR414
BGLY416
BMET417
BGLY418
BGLN448
BGLY449
BHOH701
BHOH777
BHOH780

site_idAC4
Number of Residues6
Detailsbinding site for residue K B 602
ChainResidue
BGLY329
BGLY331
BCYS334
BGLU507
BGLY508
BGLY509

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
ALEU324-THR336

226707

PDB entries from 2024-10-30

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