Structure of PDB 1fae Chain A

Receptor sequence
>1faeA (length=629) Species: 1521 (Ruminiclostridium cellulolyticum) [Search protein sequence]
ASSPANKVYQDRFESMYSKIKDPANGYFSEQGIPYHSIETLMVEAPDYGH
VTTSEAMSYYMWLEAMHGRFSGDFTGFDKSWSVTEQYLIPTEKDQPNTSM
SRYDANKPATYAPEFQDPSKYPSPLDTSQPVGRDPINSQLTSAYGTSMLY
GMHWILDVDNWYGFGARADGTSKPSYINTFQRGEQESTWETIPQPCWDEH
KFGGQYGFLDLFTKDTGTPAKQFKYTNAPDADARAVQATYWADQWAKEQG
KSVSTSVGKATKMGDYLRYSFFDKYFRKIGQPSQAGTGYDAAHYLLSWYY
AWGGGIDSTWSWIIGSSHNHFGYQNPFAAWVLSTDANFKPKSSNGASDWA
KSLDRQLEFYQWLQSAEGAIAGGATNSWNGRYEAVPSGTSTFYGMGYVEN
PVYADPGSNTWFGMQVWSMQRVAELYYKTGDARAKKLLDKWAKWINGEIK
FNADGTFQIPSTIDWEGQPDTWNPTQGYTGNANLHVKVVNYGTDLGCASS
LANTLTYYAAKSGDETSRQNAQKLLDAMWNNYSDSKGISTVEQRGDYHRF
LDQEVFVPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPEWQTMVAALQAG
QVPTQRLHRFWAQSEFAVANGVYAILFPD
3D structure
PDB1fae Crystal Structures of the Cellulase Cel48F in Complex with Inhibitors and Substrates Give Insights Into its Processive Action
ChainA
Resolution2.0 Å
3D
structure
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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 GLC A E44 D494 R609 E44 D494 R609
BS02 GLC A H36 E44 E55 W411 W417 W611 H36 E44 E55 W411 W417 W611
BS03 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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1fae, PDBe:1fae, PDBj:1fae
PDBsum1fae
PubMed10985769
UniProtP37698|GUNF_RUMCH Endoglucanase F (Gene Name=celCCF)

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