Structure of PDB 4a05 Chain A

Receptor sequence
>4a05A (length=360) Species: 209285 (Thermochaetoides thermophila) [Search protein sequence]
YNGNPFSGVQLWANTYYSSEVHTLAIPSLSPELAAKAAKVAEVPSFQWLD
RNVTVDTLFSGTLAEIRAANQRGANPPYAGIFVVYDLPDRDCAAAASNGE
WSIANNGANNYKRYIDRIRELLIQYSDIRTILVIEPDSLANMVTNMNVQK
CSNAASTYKELTVYALKQLNLPHVAMYMDAGHAGWLGWPANIQPAAELFA
QIYRDAGRPAAVRGLATNVANYNAWSIASPPSYTSPNPNYDEKHYIEAFA
PLLRNQGFDAKFIVDTGRNGKQPTGQLEWGHWCNVKGTGFGVRPTANTGH
ELVDAFVWVKPGGESDGTSDTSAARYDYHCGLSDALTPAPEAGQWFQAYF
EQLLINANPP
3D structure
PDB4a05 Structure of the Catalytic Core Module of the Chaetomium Thermophilum Family Gh6 Cellobiohydrolase Cel6A.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y200 R205 D206 S212 D252 D431
Catalytic site (residue number reindexed from 1) Y85 R90 D91 S97 D137 D316
Enzyme Commision number 3.2.1.-
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 W163 S212 K425 P426 E429 W48 S97 K310 P311 E314
BS02 BGC A D165 R166 E429 G458 D50 R51 E314 G343
BS03 BGC A T259 G299 W300 G395 T144 G184 W185 G280
BS04 BGC A N260 H297 W300 N145 H182 W185
BS05 BGC A D206 D252 W397 D91 D137 W282
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4a05, PDBe:4a05, PDBj:4a05
PDBsum4a05
PubMed22868752
UniProtG0SD43

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