Structure of PDB 3pfx Chain A

Receptor sequence
>3pfxA (length=436) Species: 68825 (Rasamsonia emersonii) [Search protein sequence]
QQAGTATAENHPPLTWQECTAPGSCTTQNGAVVLDANWRWVHDVNGYTNC
YTGNTWDPTYCPDDETCAQNCALDGADYEGTYGVTSSGSSLKLNFVTGSN
VGSRLYLLQDDSTYQIFKLLNREFSFDVDVSNLPCGLNGALYFVAMDADG
GVSKYPNNKAGAKYGTGYCDSQCPRDLKFIDGEANVEGWQPSSNNANTGI
GDHGSCCAEMDVWEANSISNAVTPHPCDTPGQTMCSGDDCGGTYSNDRYA
GTCDPDGCDFNPYRMGNTSFYGPGKIIDTTKPFTVVTQFLTDDGTDTGTL
SEIKRFYIQNSNVIPQPNSDISGVTGNSITTEFCTAQKQAFGDTDDFSQH
GGLAKMGAAMQQGMVLVMSLWDDYAAQMLWLDSDYPTDADPTTPGIARGT
CPTDSGVPSDVESQSPNSYVTYSNIKFGPINSTFTA
3D structure
PDB3pfx Crystal structure of Cel7A from Talaromyces emersonii in complex with cellobiose
ChainA
Resolution1.2616 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
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 D256 D343 R398 D256 D343 R398
BS02 BGC A R248 D256 W380 R248 D256 W380
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3pfx, PDBe:3pfx, PDBj:3pfx
PDBsum3pfx
PubMed
UniProtQ8TFL9

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