Structure of PDB 1mve Chain A Binding Site BS01

Receptor Information
>1mve Chain A (length=243) Species: 833 (Fibrobacter succinogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVSAKDFSGAELYTLEEVQYGKFEARMKMAAASGTVSSMFLYQNGSEIAD
GRPWVEVDIEVLGKNPGSFQSNIITGKAGAQKTSEKHHAVSPAADQAFHT
YGLEWTPNYVRWTVDGQEVRKTEGGQVSNLTGTQGLRFNLWSSESAAWVG
QFDESKLPLFQFINWVKVYKYTPGQGEGGSDFTLDWTDNFDTFDGSRWGK
GDWTFDGNRVDLTDKNIYSRDGMLILALTRKGQESFNGQVPRD
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 chain1mve Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mve Crystal Structure of a Natural Circularly Permuted Jellyroll Protein: 1,3-1,4-beta-D-Glucanase from Fibrobacter succinogenes.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		N164 N189 G222
Binding residue
(residue number reindexed from 1)		N164 N189 G222
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E56 E60
Catalytic site (residue number reindexed from 1) E56 E60
Enzyme Commision number 3.2.1.73: licheninase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1mve, PDBe:1mve, PDBj:1mve
PDBsum1mve
PubMed12842475
UniProtP17989|GUB_FIBSS Beta-glucanase (Gene Name=Fisuc_2961)

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