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BioLiP

Structure of PDB 2am5 Chain A

Receptor sequence
>2am5A (length=342) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQVIA
SYGSAVTHIRQPDLSNIAVQPDHRKFQGYYKIARHYRWALGQIFHNFNYP
AAVVVEDDLEVAPDFFEYFQATYPLLKADPSLWCVSAWNDNGKEQMVDSS
KPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRKGRAC
VRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVPFTQLDLSYLQQEA
YDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGV
MDDLKSGVPRAGYRGIVTFLFRGRRVHLAPPQTWDGYDPSWT
3D structure
PDB2am5 X-ray Crystal Structures of Rabbit N-acetylglucosaminyltransferase I (GnT I) in Complex with Donor Substrate Analogues.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D213 D291
Catalytic site (residue number reindexed from 1) D108 D186
Enzyme Commision number 2.4.1.101: alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 UDP A I113 A114 C115 R117 D144 C145 I187 H190 E211 D212 G320 V321 S322 I8 A9 C10 R12 D39 C40 I82 H85 E106 D107 G215 V216 S217
BS02 GOL A R131 P138 I139 S159 A160 T162 R26 P33 I34 S54 A55 T57
BS03 GOL A Y390 G412 W439 Y442 D443 W446 Y285 G307 W334 Y337 D338 W341
BS04 GOL A P235 R303 P130 R198
Gene Ontology
Molecular Function
GO:0008375 acetylglucosaminyltransferase activity
Biological Process
GO:0006486 protein glycosylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2am5, PDBe:2am5, PDBj:2am5
PDBsum2am5
PubMed16769084
UniProtP27115|MGAT1_RABIT Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (Gene Name=MGAT1)

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