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

6K0I

Crystal Structure of UDP-glucose 4-epimerase from Bifidobacterium longum in complex with NAD+ and UDP-Glc

Functional Information from GO Data
ChainGOidnamespacecontents
A0003978molecular_functionUDP-glucose 4-epimerase activity
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006012biological_processgalactose metabolic process
A0016853molecular_functionisomerase activity
A0033499biological_processgalactose catabolic process via UDP-galactose
Functional Information from PDB Data
site_idAC1
Number of Residues33
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY8
ASER37
AGLY58
AASP59
AVAL60
APHE81
AALA82
AGLY83
ALYS85
AASN100
ASER123
AGLY11
ASER124
ATYR150
ALYS154
ATYR178
APHE179
APRO181
AUPG402
AHOH520
AHOH540
AHOH559
APHE12
AHOH604
AHOH606
AHOH622
AHOH690
AILE13
AASP32
AASN33
ATYR34
AGLY35
AASN36

site_idAC2
Number of Residues29
Detailsbinding site for residue UPG A 402
ChainResidue
ALYS85
ASER125
AALA126
ATYR150
ATYR178
APHE179
AASN180
AALA199
AASN200
ALEU201
AGLN217
AVAL218
ATYR219
AGLY230
AARG232
ATYR234
AVAL269
AARG292
AASP295
ANAD401
AHOH527
AHOH541
AHOH556
AHOH603
AHOH628
AHOH648
AHOH672
AHOH676
AHOH707

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR150

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APHE12
AASN180
AASN200
AGLN217
AARG232
AARG292
AASP32
AASP59
APHE81
AASN100
ASER125
ATYR150
ALYS154
APHE179

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon