Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QM1

Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor D67

Replaces:  4MXS
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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE IMP A 500
ChainResidue
ASER306
AGLY390
AMET391
AGLY392
AGLU416
AGLY417
C39H501
AILE307
ACYS308
AASP341
AGLY342
AGLY343
AGLY364
ASER365
ATYR388

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 39H A 501
ChainResidue
ASER23
APRO27
AALA441
AGLY444
ATYR445
BMET391
BMET397
BGLU416
BIMP500

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IMP B 500
ChainResidue
A39H501
BALA49
BMET51
BGLY305
BSER306
BILE307
BCYS308
BASP341
BGLY342
BGLY343
BGLY364
BSER365
BTYR388
BGLY390
BMET391
BGLY392
BGLU416
BGLY417
BHOH603

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 39H B 501
ChainResidue
BSER23
BVAL25
BLEU26
BGLY444
BTYR445
DALA253
DMET391
DGLU416
DIMP500

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 39H C 501
ChainResidue
AALA253
ASER257
AMET397
AGLU416
AIMP500
CSER23
CVAL25
CLEU26
CALA441
CGLY444

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE IMP C 502
ChainResidue
CALA49
CMET51
CSER306
CILE307
CCYS308
CASP341
CGLY342
CGLY343
CGLY364
CSER365
CTYR388
CGLY390
CMET391
CGLY392
CGLU416
CGLY417
C39H503

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 39H C 503
ChainResidue
CALA253
CHIS254
CMET391
CGLU416
CIMP502
DSER23
DALA441
DGLY444
DTYR445

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE IMP D 500
ChainResidue
DTYR388
DGLY390
DMET391
DGLY392
DGLU416
DGLY417
B39H501
DMET51
DGLY305
DSER306
DILE307
DCYS308
DASP341
DGLY342
DGLY343
DGLY364
DSER365

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL298-THR310

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon