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4WLZ

Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with manganese and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
B0035252molecular_functionUDP-xylosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MN A 401
ChainResidue
AASP225
AASP227
AHIS382
AUDP402

site_idAC2
Number of Residues13
Detailsbinding site for residue UDP A 402
ChainResidue
ALEU226
AASP227
AHIS382
AASN384
ACYS385
AMN401
BASP361
BHIS362
AMET103
APHE104
ATHR105
ALEU113
AASP225

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG261
AARG268
ATYR364
BSER195

site_idAC4
Number of Residues4
Detailsbinding site for residue MN B 401
ChainResidue
BASP225
BASP227
BHIS382
BUDP402

site_idAC5
Number of Residues14
Detailsbinding site for residue UDP B 402
ChainResidue
ATRP358
AASP361
AHIS362
BMET103
BPHE104
BTHR105
BLEU113
BLYS116
BASP225
BLEU226
BASP227
BASN384
BCYS385
BMN401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:26414444, ECO:0007744|PDB:4WNH
ChainResidueDetails
AMET103
BGLN330
ALEU226
ASER289
ALEU327
AGLN330
BMET103
BLEU226
BSER289
BLEU327

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26414444, ECO:0007744|PDB:4WLM, ECO:0007744|PDB:4WLZ, ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB, ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK, ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH
ChainResidueDetails
AASP225
AASP227
AHIS382
BASP225
BASP227
BHIS382

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26414444, ECO:0007744|PDB:4WM0, ECO:0007744|PDB:4WNH
ChainResidueDetails
ATRP359
AASN384
BTRP359
BASN384

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PDB entries from 2024-09-04

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