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BioLiP

Structure of PDB 1hfy Chain B Binding Site BS01

Receptor Information
>1hfy Chain B (length=120) Species: 9925 (Capra hircus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEY
GLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVG
INYWLAHKALCSEKLDQWLC
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1hfy Chain B Residue 124 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1hfy Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		K79 D82 D84 D87 D88
Binding residue
(residue number reindexed from 1)		K79 D82 D84 D87 D88
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T33 N45 S47 E49 N56
Catalytic site (residue number reindexed from 1) T33 N45 S47 E49 N56
Enzyme Commision number 2.4.1.22: lactose synthase.
Gene Ontology
Molecular Function
GO:0003796 lysozyme activity
GO:0004461 lactose synthase activity
GO:0005509 calcium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0005989 lactose biosynthetic process
GO:0050829 defense response to Gram-negative bacterium
GO:0050830 defense response to Gram-positive bacterium
Cellular Component
GO:0005576 extracellular region
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hfy, PDBe:1hfy, PDBj:1hfy
PDBsum1hfy
PubMed8805552
UniProtP00712|LALBA_CAPHI Alpha-lactalbumin (Gene Name=LALBA)

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