Structure of PDB 1cen Chain A

Receptor sequence
>1cenA (length=334) Species: 1515 (Acetivibrio thermocellus) [Search protein sequence]
MVSFKAGINLGGWISQYQVFSKEHFDTFITEKDIETIAEAGFDHVRLPFD
YPIIESDDNVGEYKEDGLSYIDRCLEWCKKYNLGLVLDMHHAPGYTSTLF
EDPNQQKRFVDIWRFLAKRYINEREHIAFELLNQVVEPDSTRWNKLMLEC
IKAIREIDSTMWLYIGGNNYNSPDELKNLADIDDDYIVYNFHFYNPFFFT
HQKAHWSESAMAYNRTVKYPGQYEGIEEFVKNNPKYSFMMELNNLKLNKE
LLRKDLKPAIEFREKKKCKLYCGEFGVIAIADLESRIKWHEDYISLLEEY
DIGGAVWNYKKMDFEIYNEDRKPVSQELVNILAR
3D structure
PDB1cen The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q140 E280
Catalytic site (residue number reindexed from 1) Q134 E274
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 A H90 Q140 Y200 H207 W212 E280 W313 F320 H90 Q134 Y194 H201 W206 E274 W307 F314
BS02 BGC A Q16 W212 M318 F320 Q16 W206 M312 F314
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0009251 glucan catabolic process
GO:0030245 cellulose catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0009986 cell surface

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1cen, PDBe:1cen, PDBj:1cen
PDBsum1cen
PubMed8632467
UniProtP0C2S3|GUNC_ACETH Endoglucanase C (Gene Name=celC)

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