Structure of PDB 1qk0 Chain A

Receptor sequence
>1qk0A (length=363) Species: 51453 (Trichoderma reesei) [Search protein sequence]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFM
WLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGE
YSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPK
CANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIG
PLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTG
DSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAY
FVQLLTNANPSFL
3D structure
PDB1qk0 Crystallographic Evidence for Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase Cel6A from Trichoderma Reesei
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 XYP A Y169 K395 D401 Y85 K311 D317
BS02 BGC A W135 D137 K395 P396 E399 W51 D53 K311 P312 E315
BS03 MAN A T97 N161 T13 N77
BS04 MAN A Y103 S106 Y19 S22
BS05 MAN A S109 A125 A128 S25 A41 A44
BS06 MAN A S106 S110 S22 S26
BS07 MAN A S115 Q432 S31 Q348
BS08 MAN A G118 T122 G34 T38
BS09 IOB A A178 D221 W367 A94 D137 W283
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1qk0, PDBe:1qk0, PDBj:1qk0
PDBsum1qk0
PubMed10508787
UniProtP07987|GUX2_HYPJE Exoglucanase 2 (Gene Name=cbh2)

[Back to BioLiP]