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4XTD

Structure of the covalent intermediate E-XMP* of the IMP dehydrogenase of Ashbya gossypii

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 Residues25
Detailsbinding site for residue IMP A 601
ChainResidue
ASER74
AASP367
AGLY368
AGLY369
AMET388
AGLY390
AGLY391
ATYR414
AGLY416
AMET417
AGLY418
AMET76
AGLN448
AGLY449
AHOH704
AHOH740
AHOH745
AHOH759
AASN306
AARG325
AGLY331
ASER332
AILE333
ACYS334
ATHR336

site_idAC2
Number of Residues24
Detailsbinding site for residue IMP B 601
ChainResidue
BSER74
BMET76
BASN306
BARG325
BGLY331
BSER332
BILE333
BCYS334
BTHR336
BASP367
BGLY368
BGLY369
BMET388
BGLY390
BGLY391
BTYR414
BGLY416
BMET417
BGLY418
BGLN448
BGLY449
BHOH734
BHOH735
BHOH739

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

237735

PDB entries from 2025-06-18

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