Structure of PDB 2ovw Chain B

Receptor sequence
>2ovwB (length=398) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
QTPDKAKEQHPKLETYRCTKASGCKKQTNYIVADAGIHGIRQKNGAGCGD
WGQKPNATACPDEASCAKNCILSGMDSNAYKNAGITTSGNKLRLQQLINN
QLVSPRVYLLEENKKKYEMLHLTGTEFSFDVEMEKLPCGMNGALYLSEMP
QDGGKSTSRNSKAGAYYGAGYCDAQCYVTPFINGVGNIKGQGVCCNELDI
WEANSRATHIAPHPCSKPGLYGCTGDECGSSGICDKAGCGWNHNRINVTD
FYGRGKQYKVDSTRKFTVTSQFVANKQGDLIELHRHYIQDNKVIESAVVN
ISGPPKINFINDKYCAATGANEYMRLGGTKQMGDAMSRGMVLAMSVWWSE
GDFMAWLDQGVAGPCDATEGDPKNIVKVQPNPEVTFSNIRIGEIGSTS
3D structure
PDB2ovw Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
ChainB
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) E197 D199 E202 H213
Catalytic site (residue number reindexed from 1) E197 D199 E202 H213
Enzyme Commision number 3.2.1.4: cellulase.
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 B A143 Y145 D173 Q175 E197 D199 E202 H213 W347 A143 Y145 D173 Q175 E197 D199 E202 H213 W347
BS02 BGC B R106 Y145 S345 W347 R106 Y145 S345 W347
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
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:2ovw, PDBe:2ovw, PDBj:2ovw
PDBsum2ovw
PubMed9153432
UniProtP46237|GUNC_FUSOX Endoglucanase type C

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