Structure of PDB 4ax6 Chain A

Receptor sequence
>4ax6A (length=363) Species: 51453 (Trichoderma reesei) [Search protein sequence]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFM
WLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGE
YSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPASLANLVTNLGTPK
CANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIG
PLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTG
DSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAY
FVQLLTNANPSFL
3D structure
PDB4ax6 Rational Design, Synthesis, Evaluation and Enzyme-Substrate Structures of Improved Fluorogenic Substrates for Family 6 Glycoside Hydrolases.
ChainA
Resolution2.3 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 W135 Y169 K395 D401 W51 Y85 K311 D317
BS02 BGC A W135 D137 S181 K395 E399 W51 D53 S97 K311 E315
BS03 MAN A Y103 S106 E107 Y19 S22 E23
BS04 MAN A A105 S109 A125 A21 S25 A41
BS05 MAN A S106 S110 S22 S26
BS06 MAN A G118 T122 G34 T38
BS07 UWU A A177 H266 W269 A304 W367 A93 H182 W185 A220 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

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Molecular Function
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Biological Process
External links
PDB RCSB:4ax6, PDBe:4ax6, PDBj:4ax6
PDBsum4ax6
PubMed23137336
UniProtP07987|GUX2_HYPJE Exoglucanase 2 (Gene Name=cbh2)

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