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2OYM

Endo-glycoceramidase II from Rhodococcus sp.: five-membered iminocyclitol complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 601
ChainResidue
AASN222
AVAL225
AHOH705
AHOH733
AHOH775
AHOH788

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 601
ChainResidue
BHOH718
BHOH766
BHOH798
BASN222
BVAL225
BHOH707

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MNI A 600
ChainResidue
ALYS66
AHIS135
AASP137
AGLU179
ATYR182
AASN232
AGLU233
APHE235
ATYR306
AGLU351
ATRP382
AHOH877
AHOH964

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MNI B 600
ChainResidue
BLYS66
BHIS135
BASP137
BTRP178
BGLU179
BTYR182
BASN232
BGLU233
BPHE235
BTYR306
BGLU351
BTRP382
BHOH797
BHOH852

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VAYDLMNEPF
ChainResidueDetails
AVAL226-PHE235

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AHIS304
ATYR306
AGLU233
AGLU351
AASN232

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BHIS304
BTYR306
BGLU233
BGLU351
BASN232

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AGLU351
AARG93
AGLU233

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BGLU351
BARG93
BGLU233

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PDB entries from 2026-02-18

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