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1KVQ

UDP-GALACTOSE 4-EPIMERASE COMPLEXED WITH UDP-PHENOL

Functional Information from GO Data
ChainGOidnamespacecontents
A0003978molecular_functionUDP-glucose 4-epimerase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006012biological_processgalactose metabolic process
A0009242biological_processcolanic acid biosynthetic process
A0016853molecular_functionisomerase activity
A0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
A0033499biological_processgalactose catabolic process via UDP-galactose
A0042802molecular_functionidentical protein binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 410
ChainResidue
AGLN91
AHOH519
AHOH520
AHOH522
AHOH523
AHOH524

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 411
ChainResidue
AHOH610
AHOH801
AGLN334
AHOH608
AHOH609

site_idAC3
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 340
ChainResidue
AGLY7
AGLY10
ATYR11
AILE12
AASP31
AASN32
ALEU33
ACYS34
AASN35
ASER36
AGLY57
AASP58
AILE59
APHE80
AALA81
AGLY82
ALYS84
AASN99
ASER122
ASER123
ATYR149
ALYS153
ATYR177
APRO180
AUPG341
AHOH432
AHOH433
AHOH439
AHOH455
AHOH494
AHOH591

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE UPG A 341
ChainResidue
AALA124
AALA125
ATYR149
ATYR177
APHE178
AASN179
AASN198
AASN199
ALEU200
ALEU215
AALA216
AILE217
APHE218
AGLY229
AARG231
ATYR233
AARG292
AASP295
ATYR299
ANAD340
AHOH496
AHOH502
AHOH590
AHOH617
AHOH629
AHOH698
AHOH787

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 420
ChainResidue
ASER214
AASN285
ATYR286
AHIS287
AHOH623
AHOH686
AHOH692

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8611497
ChainResidueDetails
ATYR149

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12019271, ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497, ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134, ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498, ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982
ChainResidueDetails
ATYR11
AASP31
AASP58
APHE80
AASN99
ALYS153
APHE178

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AALA124
ATYR149
AASN179
AASN199
AALA216
AARG231
AARG292
ATYR299

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
AASN100
ATHR126
ATYR149
ALYS153

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
AGLN146
ALYS153

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR149
ALYS153

site_idMCSA1
Number of Residues3
DetailsM-CSA 188
ChainResidueDetails
AALA124activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ATYR149hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS153activator, hydrogen bond donor

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PDB entries from 2024-07-10

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