Structure of PDB 6xpw Chain E Binding Site BS01

Receptor Information

>6xpw Chain E (length=157) Species: 330879 (Aspergillus fumigatus Af293)

HHGSMSNEQTFIAIKPDGVQRGLIGPIISRFENRGFKLVAMKLVSPPQSQ
LEQHYADLSDKPFFKGLVSYMLSGPICAMVWEGRDVVKTGRTILGATNPL
ASAPGTIRGDFAIDVGRNVCHGSDSVENAKKEIALWFKPEELISWKSATF
DWVYEKA

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 6xpw Chain E Residue 201

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6xpw Nucleoside selectivity of Aspergillus fumigatus nucleoside-diphosphate kinase.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): K11 N114 H117
• Binding residue (residue number reindexed from 1): K15 N118 H121
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K11 Y51 N114 H117 E128
• Catalytic site (residue number reindexed from 1): K15 Y55 N118 H121 E132
• Enzyme Commision number: 2.7.4.6: nucleoside-diphosphate kinase.

Gene Ontology

Molecular Function

• GO:0004550 nucleoside diphosphate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006183 GTP biosynthetic process
• GO:0006228 UTP biosynthetic process
• GO:0006241 CTP biosynthetic process
• GO:0009117 nucleotide metabolic process
• GO:0009142 nucleoside triphosphate biosynthetic process
• GO:0016310 phosphorylation

External links

• PDB: RCSB:6xpw, PDBe:6xpw, PDBj:6xpw
• PDBsum: 6xpw
• PubMed: 33089641
• UniProt: Q7Z8P9|NDK_ASPFU Nucleoside diphosphate kinase (Gene Name=ndk1)