Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3USB

Crystal Structure of Bacillus anthracis Inosine Monophosphate Dehydrogenase in the complex with IMP

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
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE IMP A 500
ChainResidue
AALA49
AMSE362
AGLY364
ASER365
AHOH559
AHOH561
AHOH617
AHOH640
AHOH728
AMSE51
AGLY305
ASER306
AILE307
ACYS308
AASP341
AGLY342
AGLY343

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG65
AARG119
ALYS202
ALYS206

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
APRO27
AHIS254
AALA441
ATYR445
AHOH692

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AGLU9
ATHR322
AHOH601
AHOH744

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE IMP B 500
ChainResidue
BALA49
BSER306
BILE307
BCYS308
BASP341
BGLY342
BGLY343
BMSE362
BGLY364
BSER365
BHOH544
BHOH574
BHOH631
BHOH632
BHOH635

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 501
ChainResidue
BSER23
BPRO27
BHIS254
BALA441
BGLY444
BTYR445

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BLYS8
BGLU9
BASP326
BHOH522
BHOH604
BHOH643

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BPHE6
BLEU11
BTHR322
BHOH522

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BTHR12
BPRO304
BGLN320

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

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon