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
PDB2bvt The Structure and Characterization of a Modular Endo-Beta-1,4-Mannanase from Cellulomonas Fimi
ChainB
Resolution2.9 Å
3D
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
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)		 Binding affinity
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
View graph for
Biological Process
External links
PDB RCSB:2bvt, PDBe:2bvt, PDBj:2bvt
PDBsum2bvt
PubMed16171384
UniProtQ9XCV5

[Back to BioLiP]