Structure of PDB 1hgw Chain A

Receptor sequence
>1hgwA (length=363) Species: 51453 (Trichoderma reesei) [Search protein sequence]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFM
WLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRACAALASNGE
YSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPK
CANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIG
PLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTG
DSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAY
FVQLLTNANPSFL
3D structure
PDB1hgw The Active Site of Cellobiohydrolase Cel6A from Trichoderma Reesei: The Roles of Aspartic Acids D221 and D175
ChainA
Resolution2.1 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 A175 S181 D221 D401
Catalytic site (residue number reindexed from 1) Y85 R90 A91 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 MAN A T97 N161 T13 N77
BS02 MAN A Y103 S106 Y19 S22
BS03 MAN A S109 A125 S25 A41
BS04 MAN A S106 S110 S22 S26
BS05 MAN A S115 Q432 S31 Q348
BS06 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:1hgw, PDBe:1hgw, PDBj:1hgw
PDBsum1hgw
PubMed12188666
UniProtP07987|GUX2_HYPJE Exoglucanase 2 (Gene Name=cbh2)

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