Structure of PDB 4gyf Chain A Binding Site BS04

Receptor Information
>4gyf Chain A (length=263) Species: 272623 (Lactococcus lactis subsp. lactis Il1403) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLKKLDYHFHSHFSADSEELPRKHVTEAIAHGLEEICFTEHRDFYFPGMD
FSLNLPEYFQEINQLQAEFKDKIKIKIGLEMGIDLRFKSEINQFIDSAPF
DFVIASVHEIGDIEVYDGTEFYLQKTKEEAQREYLLACLDVVQNFENYNS
FGHLDYVARYGPYTDKSIKFAENREILFEILRALASKEKALEINTRLFDD
PKTEQFYSDLLINFKRLGGKFITLGTDSHIAKRDWLSIHKARTLIKKAGF
HELATFSGMKIDK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4gyf Chain A Residue 304 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4gyf Crystal structure of histidinol phosphate phosphatase (HISK) from Lactococcus lactis subsp. lactis Il1403 complexed with ZN, L-histidinol and phosphate
Resolution1.647 Å
Binding residue
(original residue number in PDB)
H32 H240
Binding residue
(residue number reindexed from 1)
H31 H239
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.15: histidinol-phosphatase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004401 histidinol-phosphatase activity
GO:0016787 hydrolase activity
Biological Process
GO:0000105 L-histidine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4gyf, PDBe:4gyf, PDBj:4gyf
PDBsum4gyf
PubMed
UniProtQ02150|HIS9_LACLA Histidinol-phosphatase (Gene Name=hisK)

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