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4GLL

Crystal structure of human UDP-xylose synthase.

Replaces:  4EF7
Functional Information from GO Data
ChainGOidnamespacecontents
A0042732biological_processD-xylose metabolic process
A0070403molecular_functionNAD+ binding
B0042732biological_processD-xylose metabolic process
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD A 800
ChainResidue
AGLY95
ATHR123
AGLY124
AHIS143
AASP144
AVAL145
ALEU159
AALA160
ASER161
AALA163
ATHR178
AALA97
ASER201
ATYR231
ALYS235
AILE258
ATHR261
AHIS267
AHOH940
AGLY98
APHE99
AVAL100
AASP119
AASN120
APHE121
APHE122

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GAI A 801
ChainResidue
ATHR288
ATYR290
AILE331
AASP356

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
ASER203
APHE259
AASN260
AGLN359
AARG361

site_idAC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD B 501
ChainResidue
BGLY95
BGLY98
BPHE99
BVAL100
BASP119
BASN120
BPHE121
BPHE122
BTHR123
BGLY124
BHIS143
BASP144
BVAL145
BLEU159
BALA160
BSER161
BPRO162
BALA163
BLYS174
BTHR178
BALA200
BTHR202
BTYR231
BLYS235
BILE258
BPHE259
BASN260
BTHR261
BHIS267
BARG272
BHOH608

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GAI B 502
ChainResidue
BTHR288
BTYR290
BASP356

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BTYR150
BARG192
BTYR290
BSER292
BGLY293
BSER294
BGLN295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23656592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25521717","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22810237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25521717","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B69","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4M55","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25521717","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LK3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25521717","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4M55","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22810237","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B69","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25521717","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4M55","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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