BioLiP

Structure of PDB 2bvt Chain B

Receptor sequence

>2bvtB (length=451) Species: 1708 (Cellulomonas fimi) [Search protein sequence]

TIAIVDADATAETRSLLSYLDGVRGEGILFGHQHTTSFGLTTGPTDGTTS
DVKNVTGDFPAVFGWDTLIIEGNERPGLAENTRDENIALFADYIRKADAI
GGVNTVSAHVENFVTGGSFYDTSGDTLRAVLPGGSHHAELVAYLDDIAEL
ADASRRDDGTLIPIVFRPWHENAGSWFWWGAAYGSPGEYQELYRFTVEYL
RDVKGVSNFLYAWGPGGGFGGNRDVYLRTYPGDAFVDVLGLDTYDSTGSD
AFLAGLVADLRMIAEIADEKGKVSAFTEFGVSGGVGTNGSSPAQWFTKVL
AAIKADPVASRNAYMETWANFDAGQHFVPVPGDALLEDFQAYAADPFTLF
ASEVTGAFDRTVAAAPAQPVVHIASPADGARVASAPTTVRVRVGGTDVQS
VTVEVAQVVDTLDLAYDGALWWTAPWSPYTVTATATTAAGTLDVTNEVAA
A

3D structure

PDB

2bvt The Structure and Characterization of a Modular Endo-Beta-1,4-Mannanase from Cellulomonas Fimi

Chain

Resolution

2.9 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

3.2.1.78: mannan endo-1,4-beta-mannosidase.

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)
BS01	BMA	B	E78 W322 Q329	E74 W318 Q325
BS02	BMA	B	N77 E78	N73 E74
BS03	CAC	B	H113 H174 E175 E282 W322	H109 H170 E171 E278 W318

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016985	mannan endo-1,4-beta-mannosidase activity

	Biological Process
GO:0006080	substituted mannan metabolic process

View graph for
Molecular Function

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Biological Process

PDB	RCSB:2bvt, PDBe:2bvt, PDBj:2bvt
PDBsum	2bvt
PubMed	16171384
UniProt	Q9XCV5