Structure of PDB 1l1y Chain D

Receptor sequence
>1l1yD (length=642) Species: 1515 (Acetivibrio thermocellus) [Search protein sequence]
GPTKAPTKDGTSYKDLFLELYGKIKDPKNGYFSPDEGIPYHSIETLIVEA
PDYGHVTTSEAFSYYVWLEAMYGNLTGNWSGVETAWKVMEDWIIPDSTEQ
PGMSSYNPNSPATYADEYEDPSYYPSELKFDTVRVGSDPVHNDLVSAYGP
NMYLMHWLMDVDNWYGFGTGTRATFINTFQRGEQESTWETIPHPSIEEFK
YGGPNGFLDLFTKDRSYAKQWRYTNAPDAEGRAIQAVYWANKWAKEQGKG
SAVASVVSKAAKMGDFLRNDMFDKYFMKIGAQDKTPATGYDSAHYLMAWY
TAWGGGIGASWAWKIGCSHAHFGYQNPFQGWVSATQSDFAPKSSNGKRDW
TTSYKRQLEFYQWLQSAEGGIAGGATNSWNGRYEKYPAGTSTFYGMAYVP
HPVYADPGSNQWFGFQAWSMQRVMEYYLETGDSSVKNLIKKWVDWVMSEI
KLYDDGTFAIPSDLEWSGQPDTWTGTYTGNPNLHVRVTSYGTDLGVAGSL
ANALATYAAATERWEGKLDTKARDMAAELVNRAWYNFYCSEGKGVVTEEA
RADYKRFFEQEVYVPAGWSGTMPNGDKIQPGIKFIDIRTKYRQDPYYDIV
YQAYLRGEAPVLNYHRFWHEVDLAVAMGVLATYFPDMTYKVP
3D structure
PDB1l1y The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome.
ChainD
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.176: cellulose 1,4-beta-cellobiosidase (reducing end).
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 D E76 D520 R643 H646 E49 D493 R616 H619
BS02 BGC D H68 E76 E87 W439 W445 W645 H41 E49 E60 W412 W418 W618
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
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:1l1y, PDBe:1l1y, PDBj:1l1y
PDBsum1l1y
PubMed12096911
UniProtP0C2S5|GUNS_ACETH Cellulose 1,4-beta-cellobiosidase (reducing end) CelS (Gene Name=celS)

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