Structure of PDB 1mve Chain A

Receptor sequence
>1mveA (length=243) Species: 833 (Fibrobacter succinogenes) [Search protein sequence]
MVSAKDFSGAELYTLEEVQYGKFEARMKMAAASGTVSSMFLYQNGSEIAD
GRPWVEVDIEVLGKNPGSFQSNIITGKAGAQKTSEKHHAVSPAADQAFHT
YGLEWTPNYVRWTVDGQEVRKTEGGQVSNLTGTQGLRFNLWSSESAAWVG
QFDESKLPLFQFINWVKVYKYTPGQGEGGSDFTLDWTDNFDTFDGSRWGK
GDWTFDGNRVDLTDKNIYSRDGMLILALTRKGQESFNGQVPRD
3D structure
PDB1mve Crystal Structure of a Natural Circularly Permuted Jellyroll Protein: 1,3-1,4-beta-D-Glucanase from Fibrobacter succinogenes.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 CA A N164 N189 G222 N164 N189 G222
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

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

[Back to BioLiP]