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6JYZ

Crystal structure of endogalactoceramidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PE4 A 501
ChainResidue
AILE181
AHOH643
AHOH1046
AHOH1110
AGLN184
AALA187
APRO242
APHE283
APHE285
AASP286
AALA287
AVAL312

site_idAC2
Number of Residues2
Detailsbinding site for residue IPA A 502
ChainResidue
AARG423
AGLU445

site_idAC3
Number of Residues2
Detailsbinding site for residue IPA A 503
ChainResidue
AASP286
AHOH911

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 504
ChainResidue
APHE110
AALA116
AARG215
AHOH698
AHOH717
AHOH864
AHOH914

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 505
ChainResidue
AGLU430
AGLY435
AARG437
ATHR486

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. DVAltRVDGGWRLI
ChainResidueDetails
AASP463-ILE476

site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VGYDLLNEPN
ChainResidueDetails
AVAL227-ASN236

227344

PDB entries from 2024-11-13

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