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3KHJ

C. parvum inosine monophosphate dehydrogenase bound by inhibitor C64

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
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0006164biological_processpurine nucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0006164biological_processpurine nucleotide biosynthetic process
D0016491molecular_functionoxidoreductase activity
E0003824molecular_functioncatalytic activity
E0003938molecular_functionIMP dehydrogenase activity
E0006164biological_processpurine nucleotide biosynthetic process
E0016491molecular_functionoxidoreductase activity
F0003824molecular_functioncatalytic activity
F0003938molecular_functionIMP dehydrogenase activity
F0006164biological_processpurine nucleotide biosynthetic process
F0016491molecular_functionoxidoreductase activity
G0003824molecular_functioncatalytic activity
G0003938molecular_functionIMP dehydrogenase activity
G0006164biological_processpurine nucleotide biosynthetic process
G0016491molecular_functionoxidoreductase activity
H0003824molecular_functioncatalytic activity
H0003938molecular_functionIMP dehydrogenase activity
H0006164biological_processpurine nucleotide biosynthetic process
H0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IMP A 801
ChainResidue
ASER48
AGLY275
ASER276
AHOH401
AHOH409
AMET50
AGLY216
ASER217
AILE218
AASP252
AGLY253
AGLY254
AMET273

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE IMP B 804
ChainResidue
BSER48
BMET50
BGLY216
BSER217
BILE218
BCYS219
BASP252
BGLY253
BGLY254
BGLY275
BSER276
BTYR299
BGLY301
BMET302
BGLY303
BGLU329
BGLY330
BHOH406
BHOH414
BHOH419
BC64901

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE C64 B 901
ChainResidue
ASER354
AGLY357
ATYR358
BALA165
BMET302
BGLY303
BGLU329
BIMP804

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE IMP C 803
ChainResidue
CSER48
CMET50
CGLY216
CSER217
CILE218
CCYS219
CASP252
CGLY253
CGLY254
CMET273
CGLY275
CSER276
CTYR299
CHOH401
CHOH408
CHOH431

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IMP D 802
ChainResidue
DSER48
DMET50
DGLY216
DSER217
DILE218
DCYS219
DASP252
DGLY253
DGLY254
DMET273
DGLY275
DSER276
DTYR299
DGLY301
DMET302
DGLY303
DGLU329
DGLY330
DHOH408
DHOH410
DHOH430
DC64902

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 401
ChainResidue
DGLU287
DLYS297
DTYR298

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE C64 D 902
ChainResidue
CSER354
CGLY357
CTYR358
DALA165
DMET302
DGLY303
DMET308
DMET326
DGLU329
DIMP802

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE IMP E 805
ChainResidue
EGLY275
ESER276
ESER48
ETHR220
ETHR221
EASP252
EGLY253
EGLY254

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IMP F 808
ChainResidue
FSER48
FMET50
FHOH111
FGLY216
FSER217
FASP252
FGLY253
FGLY254
FMET273
FILE274
FGLY275
FSER276

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IMP G 807
ChainResidue
GSER48
GSER164
GALA165
GASN191
GGLY216
GASP252
GGLY254
GILE255
GGLY275
GSER276

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IMP H 806
ChainResidue
HSER48
HMET50
HGLY216
HSER217
HILE218
HCYS219
HASP252
HGLY253
HGLY254
HGLY275
HSER276
HTYR299
HGLY301
HMET302
HGLY303
HGLU329
HGLY330
HHOH410
HC64903

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE C64 H 903
ChainResidue
GPRO26
GGLY357
GTYR358
HALA165
HHIS166
HMET302
HGLY303
HMET308
HMET326
HGLU329
HIMP806

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSICtT
ChainResidueDetails
AILE209-THR221

223166

PDB entries from 2024-07-31

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