Structure of PDB 1rq5 Chain A

Receptor sequence
>1rq5A (length=602) Species: 1515 (Acetivibrio thermocellus) [Search protein sequence]
ILPQPDVRVNQVGYLPEGKKVATVVCNSTQPVKWQLKNAAGVVVLEGYTE
PKGLDKDSQDYVHWLDFSDFATEGIGYYFELPTVNSPTNYSHPFDIRKDI
YTQMKYDALAFFYHKRSGIPIEMPYAGGEQWTRPAGHIGIEPNKGDTNVP
TWPQDDEYAGIPQKNYTKDVTGGWYDAGDHGKYVVNGGIAVWTLMNMYER
AKIRGLDNWGPYRDGGMNIPEQNNGYPDILDEARWEIEFFKKMQVTEKED
PSIAGMVHHKIHDFRWTALGMLPHEDPQPRYLRPVSTAATLNFAATLAQS
ARLWKDYDPTFAADCLEKAEIAWQAALKHPDIYAEYTPGSGGPGGGPYND
DYVGDEFYWAACELYVTTGKDEYKNYLMNSPHYLEMPAKMGGEDNGLWGC
FTWGTTQGLGTITLALVENGLPATDIQKARNNIAKAADRWLENIEEQGYR
LPIKQAEDERGGYPWGSNSFILNQMIVMGYAYDFTGDSKYLDGMFDGISY
LLGRNAMDQSYVTGYGERPLQNPHDRFWTPQTSKRFPAPPPGIISGGPNS
RFEDPTINAAVKKDTPPQKCFIDHTDSWGTNQITVNWNAPFAWVTAYLDE
QY
3D structure
PDB1rq5 Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D383 D386 Y555 Q795
Catalytic site (residue number reindexed from 1) D176 D179 Y348 Q582
Enzyme Commision number 3.2.1.-
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1rq5, PDBe:1rq5, PDBj:1rq5
PDBsum1rq5
PubMed14756552
UniProtQ59325

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