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1EK5

STRUCTURE OF HUMAN UDP-GALACTOSE 4-EPIMERASE IN COMPLEX WITH NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003974molecular_functionUDP-N-acetylglucosamine 4-epimerase activity
A0003978molecular_functionUDP-glucose 4-epimerase activity
A0005829cellular_componentcytosol
A0006012biological_processgalactose metabolic process
A0016853molecular_functionisomerase activity
A0019388biological_processgalactose catabolic process
A0033499biological_processgalactose catabolic process via UDP-galactose
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAD A 400
ChainResidue
AGLY9
AALA38
AMET65
AASP66
AILE67
APHE88
AGLY90
ALYS92
ASER130
ASER131
ATYR157
AGLY12
ALYS161
ATYR185
APHE186
APRO188
AASN206
AHOH605
AHOH606
AHOH625
AHOH631
AHOH653
ATYR13
AHOH655
AHOH656
AHOH658
AHOH660
AILE14
AASP33
AASN34
APHE35
AHIS36
AASN37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331
ChainResidueDetails
ATYR157

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193
ChainResidueDetails
AGLY12
AASP33
AASP66
APHE88
ALYS92
ALYS161
AASN206
AASN224
AARG239

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331
ChainResidueDetails
ASER132

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10801319
ChainResidueDetails
ATYR185

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193
ChainResidueDetails
AARG300

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS161
ATYR157
ASER132

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS161
ASER130
ATYR157
AASN108

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR141
ALYS161

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS161
ATYR157

222036

PDB entries from 2024-07-03

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