Structure of PDB 1nvk Chain A Binding Site BS01

Receptor Information

>1nvk Chain A (length=351) Species: 10665 (Tequatrovirus T4)

MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L

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:
  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: 1nvk Chain A Residue 700

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1nvk Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): G188 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272
• Binding residue (residue number reindexed from 1): G188 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): E22 F72 D100 R191
• Catalytic site (residue number reindexed from 1): E22 F72 D100 R191
• Enzyme Commision number: 2.4.1.27: DNA beta-glucosyltransferase.

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity
• GO:0033821 DNA beta-glucosyltransferase activity

Biological Process

• GO:0006304 DNA modification
• GO:0019049 virus-mediated perturbation of host defense response
• GO:0052170 symbiont-mediated suppression of host innate immune response
• GO:0099018 symbiont-mediated evasion of host restriction-modification system

External links

• PDB: RCSB:1nvk, PDBe:1nvk, PDBj:1nvk
• PDBsum: 1nvk
• PubMed: 12860129
• UniProt: P04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)