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4AF0

Crystal structure of cryptococcal inosine monophosphate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MOA A 1526
ChainResidue
AASP288
AGLN470
AIMP1527
ASER289
ASER290
AASN317
AGLY338
AMET339
AGLY340
AMET428
AGLY429

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP A 1527
ChainResidue
ASER86
AMET88
AASN317
AARG336
AGLY342
ASER343
AILE344
ACYS345
AASP378
AGLY379
AGLY380
AGLY401
AGLY402
ATYR425
AGLY427
AMET428
AGLY429
AGLN470
AGLY471
AMOA1526
AHOH2181
AHOH2195
AHOH2206
AHOH2208

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MOA B 1526
ChainResidue
BASP288
BSER289
BSER290
BASN317
BGLY338
BMET339
BGLY340
BMET428
BGLY429
BGLN470
BIMP1527
BHOH2163

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP B 1527
ChainResidue
BSER86
BMET88
BASN317
BARG336
BGLY342
BSER343
BILE344
BCYS345
BASP378
BGLY379
BGLY380
BGLY401
BGLY402
BTYR425
BGLY427
BMET428
BGLY429
BGLN470
BGLY471
BMOA1526
BHOH2177
BHOH2199
BHOH2201
BHOH2202

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1528
ChainResidue
BTHR4
BASN5
BPRO9
BPRO10
BHOH2003
BHOH2004

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1529
ChainResidue
BLEU25
BGLU26
BTYR28
BARG30
BGLY31
BHOH2178

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
BLEU335-THR347
ALEU335-THR347

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PDB entries from 2024-10-09

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