Structure of PDB 4au0 Chain A

Receptor sequence
>4au0A (length=363) Species: 51453 (Trichoderma reesei) [Search protein sequence]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFM
WLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGE
YSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPASLANLVTNLGTPK
CANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIG
PLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTG
DSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAY
FVQLLTNANPSFL
3D structure
PDB4au0 Rational Design, Synthesis, Evaluation and Enzyme-Substrate Structures of Improved Fluorogenic Substrates for Family 6 Glycoside Hydrolases.
ChainA
Resolution1.7 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 A221 D401
Catalytic site (residue number reindexed from 1) Y85 R90 D91 S97 A137 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 BGC A N229 H266 W269 N145 H182 W185
BS02 BGC A D175 N305 D91 N221
BS03 MAN A T97 N161 T13 N77
BS04 MAN A Y103 S106 Y19 S22
BS05 MAN A A105 S109 A125 A128 A21 S25 A41 A44
BS06 MAN A S106 S110 S22 S26
BS07 MAN A G118 T122 G34 T38
BS08 MAN A S89 G90 N91 V94 S5 G6 N7 V10
BS09 XZZ A G268 W272 Q363 W364 G365 G184 W188 Q279 W280 G281
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:4au0, PDBe:4au0, PDBj:4au0
PDBsum4au0
PubMed23137336
UniProtP07987|GUX2_HYPJE Exoglucanase 2 (Gene Name=cbh2)

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