Structure of PDB 3pfz Chain A Binding Site BS04

Receptor Information
>3pfz Chain A (length=436) Species: 68825 (Rasamsonia emersonii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QQAGTATAENHPPLTWQECTAPGSCTTQNGAVVLDANWRWVHDVNGYTNC
YTGNTWDPTYCPDDETCAQNCALDGADYEGTYGVTSSGSSLKLNFVTGSN
VGSRLYLLQDDSTYQIFKLLNREFSFDVDVSNLPCGLNGALYFVAMDADG
GVSKYPNNKAGAKYGTGYCDSQCPRDLKFIDGEANVEGWQPSSNNANTGI
GDHGSCCAEMDVWEANSISNAVTPHPCDTPGQTMCSGDDCGGTYSNDRYA
GTCDPDGCDFNPYRMGNTSFYGPGKIIDTTKPFTVVTQFLTDDGTDTGTL
SEIKRFYIQNSNVIPQPNSDISGVTGNSITTEFCTAQKQAFGDTDDFSQH
GGLAKMGAAMQQGMVLVMSLWDDYAAQMLWLDSDYPTDADPTTPGIARGT
CPTDSGVPSDVESQSPNSYVTYSNIKFGPINSTFTA
Ligand information
Ligand IDBGC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChIKeyWQZGKKKJIJFFOK-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain3pfz Chain C Residue 4 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3pfz Crystal structure of Cel7A from Talaromyces emersonii in complex with cellotetraose
Resolution1.0993 Å
Binding residue
(original residue number in PDB)		W38 Y51 N100 K178
Binding residue
(residue number reindexed from 1)		W38 Y51 N100 K178
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E209 D211 E214 H225
Catalytic site (residue number reindexed from 1) E209 D211 E214 H225
Enzyme Commision number 3.2.1.-
3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
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:3pfz, PDBe:3pfz, PDBj:3pfz
PDBsum3pfz
PubMed
UniProtQ8TFL9

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