Structure of PDB 5vcm Chain A Binding Site BS02
Receptor Information
>5vcm Chain A (length=351) Species:
9606
(Homo sapiens) [
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NLTLRYRSLVYQLNFDQTLRNVDWAPRELVLVVQVHNRPEYLRLLLDSLR
KAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFSIQLYPNEFP
GSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLH
FVWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVL
SLGTYSSRSFYGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCT
YDDYNWDWTLQYLTVSCLPKFWKVLVPQIPRIFHAGDCGCRPSTQSAQIE
SLLNNNKQYMFPETLTISEKFTVVAISPPRKNGGWGDIRDHELCKSYRRL
Q
Ligand information
Ligand ID
UDP
InChI
InChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKey
XCCTYIAWTASOJW-XVFCMESISA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.0
C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.370
O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370
O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.0
C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01
O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
Formula
C9 H14 N2 O12 P2
Name
URIDINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL130266
DrugBank
DB03435
ZINC
ZINC000004490939
PDB chain
5vcm Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
5vcm
HumanN-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite.
Resolution
1.599 Å
Binding residue
(original residue number in PDB)
Q123 H125 R127 D154 Q229 T230 E259 E260 D261 H374
Binding residue
(residue number reindexed from 1)
Q34 H36 R38 D65 Q140 T141 E170 E171 D172 H284
Annotation score
3
Enzymatic activity
Enzyme Commision number
2.4.1.143
: alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase.
Gene Ontology
Molecular Function
GO:0008455
alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
GO:0016757
glycosyltransferase activity
GO:0030145
manganese ion binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
Biological Process
GO:0006486
protein glycosylation
GO:0006487
protein N-linked glycosylation
GO:0009312
oligosaccharide biosynthetic process
GO:0018279
protein N-linked glycosylation via asparagine
GO:0019082
viral protein processing
Cellular Component
GO:0000139
Golgi membrane
GO:0005794
Golgi apparatus
GO:0005795
Golgi stack
GO:0016020
membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5vcm
,
PDBe:5vcm
,
PDBj:5vcm
PDBsum
5vcm
PubMed
29666272
UniProt
Q10469
|MGAT2_HUMAN Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (Gene Name=MGAT2)
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