Structure of PDB 1fce Chain A

Receptor sequence

>1fceA (length=629) Species: 1521 (Ruminiclostridium cellulolyticum)

ASSPANKVYQDRFESMYSKIKDPANGYFSEQGIPYHSIETLMVEAPDYGH
VTTSEAMSYYMWLEAMHGRFSGDFTGFDKSWSVTEQYLIPTEKDQPNTSM
SRYDANKPATYAPEFQDPSKYPSPLDTSQPVGRDPINSQLTSAYGTSMLY
GMHWILDVDNWYGFGARADGTSKPSYINTFQRGEQESTWETIPQPCWDEH
KFGGQYGFLDLFTKDTGTPAKQFKYTNAPDADARAVQATYWADQWAKEQG
KSVSTSVGKATKMGDYLRYSFFDKYFRKIGQPSQAGTGYDAAHYLLSWYY
AWGGGIDSTWSWIIGSSHNHFGYQNPFAAWVLSTDANFKPKSSNGASDWA
KSLDRQLEFYQWLQSAEGAIAGGATNSWNGRYEAVPSGTSTFYGMGYVEN
PVYADPGSNTWFGMQVWSMQRVAELYYKTGDARAKKLLDKWAKWINGEIK
FNADGTFQIPSTIDWEGQPDTWNPTQGYTGNANLHVKVVNYGTDLGCASS
LANTLTYYAAKSGDETSRQNAQKLLDAMWNNYSDSKGISTVEQRGDYHRF
LDQEVFVPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPEWQTMVAALQAG
QVPTQRLHRFWAQSEFAVANGVYAILFPD

3D structure

• PDB: 1fce The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A resolution.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• 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	MGL	A	T226 K274 Y299	T226 K274 Y299
BS02	SGC	A	Q181 K274	Q181 K274
BS03	BGC	A	T110 Q222 W312	T110 Q222 W312
BS04	MGL	A	Q543 G545	Q543 G545
BS05	BGC	A	E44 W411 D494 R609	E44 W411 D494 R609
BS06	BGC	A	H36 E44 E55 W411 W611	H36 E44 E55 W411 W611
BS07	CA	A	Q185 E190 D405	Q185 E190 D405

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0008810 cellulase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0030245 cellulose catabolic process

External links

• PDB: RCSB:1fce, PDBe:1fce, PDBj:1fce
• PDBsum: 1fce
• PubMed: 9755156
• UniProt: P37698|GUNF_RUMCH Endoglucanase F (Gene Name=celCCF)