Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1VF8

The Crystal Structure of Ym1 at 1.31 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005975biological_processcarbohydrate metabolic process
A0006954biological_processinflammatory response
A0008061molecular_functionchitin binding
A0009624biological_processresponse to nematode
A0010269biological_processresponse to selenium ion
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0031410cellular_componentcytoplasmic vesicle
A0048237cellular_componentrough endoplasmic reticulum lumen
A0102148molecular_functionobsolete N-acetyl-beta-D-galactosaminidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AHIS49
AGLY76
ATYR120
AMET189
ATRP339

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP117
AGLN119
ATYR191

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP117
AGLN119

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AGLN119
AASN115

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon