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2CU0

Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0009152biological_processpurine ribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0009152biological_processpurine ribonucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE XMP A 1001
ChainResidue
AMET55
AMET355
AGLY357
AASN358
ATYR381
AGLY383
AMET384
AGLY385
AGLU412
AGLY413
AHOH1005
AGLY298
AHOH1020
AHOH1024
AHOH1030
AHOH1049
AHOH1118
ASER299
AILE300
ACYS301
ATHR303
AASP334
AGLY335
AGLY336

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE XMP B 1002
ChainResidue
BALA53
BMET55
BGLY298
BSER299
BILE300
BCYS301
BTHR303
BASP334
BGLY335
BGLY336
BMET355
BGLY357
BASN358
BTYR381
BGLY383
BMET384
BGLY385
BGLU412
BGLY413
BHOH1006
BHOH1008
BHOH1014
BHOH1030

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL291-THR303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01964","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01964","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01964","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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