Structure of PDB 3pfz Chain A

Receptor sequence

>3pfzA (length=436) Species: 68825 (Rasamsonia emersonii)

QQAGTATAENHPPLTWQECTAPGSCTTQNGAVVLDANWRWVHDVNGYTNC
YTGNTWDPTYCPDDETCAQNCALDGADYEGTYGVTSSGSSLKLNFVTGSN
VGSRLYLLQDDSTYQIFKLLNREFSFDVDVSNLPCGLNGALYFVAMDADG
GVSKYPNNKAGAKYGTGYCDSQCPRDLKFIDGEANVEGWQPSSNNANTGI
GDHGSCCAEMDVWEANSISNAVTPHPCDTPGQTMCSGDDCGGTYSNDRYA
GTCDPDGCDFNPYRMGNTSFYGPGKIIDTTKPFTVVTQFLTDDGTDTGTL
SEIKRFYIQNSNVIPQPNSDISGVTGNSITTEFCTAQKQAFGDTDDFSQH
GGLAKMGAAMQQGMVLVMSLWDDYAAQMLWLDSDYPTDADPTTPGIARGT
CPTDSGVPSDVESQSPNSYVTYSNIKFGPINSTFTA

3D structure

• PDB: 3pfz Crystal structure of Cel7A from Talaromyces emersonii in complex with cellotetraose
• Chain: A
• Resolution: 1.0993 Å

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	R104 Y142 S369 W371	R104 Y142 S369 W371
BS02	BGC	A	W38 R104 D176	W38 R104 D176
BS03	BGC	A	N37 W38 V101	N37 W38 V101
BS04	BGC	A	W38 Y51 N100 K178	W38 Y51 N100 K178
BS05	BGC	A	D256 R264 D343 R398	D256 R264 D343 R398
BS06	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

External links

• PDB: RCSB:3pfz, PDBe:3pfz, PDBj:3pfz
• PDBsum: 3pfz
• UniProt: Q8TFL9