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

1EEP

2.4 A RESOLUTION CRYSTAL STRUCTURE OF BORRELIA BURGDORFERI INOSINE 5'-MONPHOSPHATE DEHYDROGENASE IN COMPLEX WITH A SULFATE ION

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AGLY263
AGLY264
AGLY285
AASN286
AHOH735

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BASN286
BHOH754
BMET50
BGLY263
BGLY264
BGLY285

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LKVGIGpGSICtT
ChainResidueDetails
ALEU219-THR231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Thioimidate intermediate => ECO:0000250|UniProtKB:P50097
ChainResidueDetails
ACYS229
BCYS229

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKI7
ChainResidueDetails
AARG325
BARG325

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P50097
ChainResidueDetails
ASER227
AASP262
AGLY285
ATYR309
AGLU340
AGLU394
ASER395
AHIS396
BASP172
BGLY222
BSER227
BASP262
BGLY285
BTYR309
BGLU340
BGLU394
BSER395
BHIS396
AASP172
AGLY222

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P50097
ChainResidueDetails
AGLY224
AGLY226
ACYS229
BGLY224
BGLY226
BCYS229

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon