Structure of PDB 1ovw Chain B

Receptor sequence
>1ovwB (length=398) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
QTPDKAKEQHPKLETYRCTKASGCKKQTNYIVADAGIHGIRQKNGAGCGD
WGQKPNATACPDEASCAKNCILSGMDSNAYKNAGITTSGNKLRLQQLINN
QLVSPRVYLLEENKKKYEMLHLTGTEFSFDVEMEKLPCGMNGALYLSEMP
QDGGKSTSRNSKAGAYYGAGYCDAQCYVTPFINGVGNIKGQGVCCNELDI
WEANSRATHIAPHPCSKPGLYGCTGDECGSSGICDKAGCGWNHNRINVTD
FYGRGKQYKVDSTRKFTVTSQFVANKQGDLIELHRHYIQDNKVIESAVVN
ISGPPKINFINDKYCAATGANEYMRLGGTKQMGDAMSRGMVLAMSVWWSE
GDFMAWLDQGVAGPCDATEGDPKNIVKVQPNPEVTFSNIRIGEIGSTS
3D structure
PDB1ovw Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group.
ChainB
Resolution2.7 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 SSG B D199 E202 H209 H213 A237 W356 D199 E202 H209 H213 A237 W356
BS02 SGC B A143 Y145 D173 Q175 E197 D199 E202 W347 A143 Y145 D173 Q175 E197 D199 E202 W347
BS03 SGC B Y145 S345 W347 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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1ovw, PDBe:1ovw, PDBj:1ovw
PDBsum1ovw
PubMed8952478
UniProtP46237|GUNC_FUSOX Endoglucanase type C

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