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4Z0G

Structure of the IMPDH from Ashbya gossypii bound to GMP

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 Residues27
Detailsbinding site for residue 5GP A 600
ChainResidue
ASER74
AASP367
AGLY369
AMET388
AGLY390
AGLY391
ATYR414
AGLY416
AMET417
AGLY418
AGLN448
AMET76
AGLY449
AGOL603
AHOH729
AHOH766
AHOH769
AHOH807
AHOH809
AHOH872
AASN306
AARG325
AGLY331
ASER332
AILE333
ACYS334
ATHR336

site_idAC2
Number of Residues14
Detailsbinding site for residue 5GP A 601
ChainResidue
AILE48
APHE50
APRO51
ASER52
ASER283
AVAL284
APHE285
AHIS473
AGLN476
AHOH718
AHOH885
AHOH911
AHOH945
BGLU295

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 602
ChainResidue
AGLY329
AGLY331
ACYS334
AGLU507
AGLY508
AGLY509

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 603
ChainResidue
AASP277
ASER278
ASER279
AASN306
AMET417
A5GP600
AHOH715
AHOH951

site_idAC5
Number of Residues27
Detailsbinding site for residue 5GP B 600
ChainResidue
BSER74
BMET76
BASN306
BARG325
BGLY331
BSER332
BILE333
BCYS334
BTHR336
BASP367
BGLY369
BMET388
BGLY390
BGLY391
BTYR414
BGLY416
BMET417
BGLY418
BGLN448
BGLY449
BGOL603
BHOH733
BHOH770
BHOH804
BHOH809
BHOH810
BHOH857

site_idAC6
Number of Residues15
Detailsbinding site for residue 5GP B 601
ChainResidue
BILE48
BPHE50
BPRO51
BSER52
BSER283
BVAL284
BPHE285
BHIS473
BGLN476
BHOH745
BHOH760
BHOH780
BHOH863
BHOH869
BHOH916

site_idAC7
Number of Residues6
Detailsbinding site for residue K B 602
ChainResidue
BCYS334
BGLU507
BGLY508
BGLY509
BGLY329
BGLY331

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL B 603
ChainResidue
BASP277
BSER278
BASN306
BMET417
B5GP600
BHOH940

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

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PDB entries from 2025-06-18

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