Structure of PDB 2bwc Chain B

Receptor sequence
>2bwcB (length=226) Species: 29549 (Rhodothermus marinus) [Search protein sequence]
TVELCGRWDARDVAGGRYRVINNVWGAETAQCIEVGLETGNFTITRADHD
NGNNVAAYPAIYFGCHWGACTSNSGLPRRVQELSDVRTSWTLTPITTGRW
NAAYDIWFSPVTNSGNGYSGGAELMIWLNWNGGVMPGGSRVATVELAGAT
WEVWYADWDWNYIAYRRTTPTTSVSELDLKAFIDDAVARGYIRPEWYLHA
VETGFELWEGGAGLRSADFSVTVQKL
3D structure
PDB2bwc Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E124 E207
Catalytic site (residue number reindexed from 1) E123 E206
Enzyme Commision number 3.2.1.4: cellulase.
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 BGC B W26 Y59 E124 W161 E207 W25 Y58 E123 W160 E206
BS02 BGC B N24 W26 H67 W68 N23 W25 H66 W67
BS03 BGC B W9 H67 W8 H66
BS04 GLC B P137 G138 W159 Y163 E207 P136 G137 W158 Y162 E206
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:2bwc, PDBe:2bwc, PDBj:2bwc
PDBsum2bwc
PubMed16343530
UniProtO33897

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