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1OMX

Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
B0016020cellular_componentmembrane
B0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
APHE171
AGLN174
APRO260
AILE314
AHOH432

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 402
ChainResidue
BHOH417
BPHE171
BGLN174
BPRO260
BILE263

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
ALYS222
ATYR223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATHR38-SER58
BTHR38-SER58

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
APRO59-LEU79
BPRO59-LEU79

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12562774
ChainResidueDetails
AMET283
BMET283

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:12562774, ECO:0007744|PDB:1ON6, ECO:0007744|PDB:1ON8
ChainResidueDetails
AGLU109
BGLY189
AASN113
AVAL138
AILE167
AGLY189
BGLU109
BASN113
BVAL138
BILE167

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12562774, ECO:0007744|PDB:1ON6
ChainResidueDetails
APRO172
BGLY282
BMET283
BMET330
ASER188
AILE190
AGLY282
AMET283
AMET330
BPRO172
BSER188
BILE190

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATRP112
BTRP112

238268

PDB entries from 2025-07-02

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