Structure of PDB 1qk2 Chain A

Receptor sequence
>1qk2A (length=363) Species: 51453 (Trichoderma reesei) [Search protein sequence]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFM
WLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGE
YSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPK
CANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIG
PLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTG
DSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAY
FVQLLTNANPSFL
3D structure
PDB1qk2 Crystallographic Evidence for Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase Cel6A from Trichoderma Reesei
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y169 R174 D175 S181 D221 D401
Catalytic site (residue number reindexed from 1) Y85 R90 D91 S97 D137 D317
Enzyme Commision number 3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-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 MGL A N229 H266 G365 N145 H182 G281
BS02 SGC A D221 W367 D137 W283
BS03 GLC A Y169 A304 K395 D401 Y85 A220 K311 D317
BS04 GLC A W135 D137 K395 E399 W51 D53 K311 E315
BS05 MAN A T87 Y88 T3 Y4
BS06 MAN A Y103 S106 Y19 S22
BS07 MAN A S109 A125 S25 A41
BS08 MAN A S106 S110 S22 S26
BS09 MAN A S115 Q432 S31 Q348
BS10 MAN A G118 T122 G34 T38
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:1qk2, PDBe:1qk2, PDBj:1qk2
PDBsum1qk2
PubMed10508787
UniProtP07987|GUX2_HYPJE Exoglucanase 2 (Gene Name=cbh2)

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