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6E58

Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
A0042783biological_processevasion of host immune response
A0043655cellular_componenthost extracellular space
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
B0042783biological_processevasion of host immune response
B0043655cellular_componenthost extracellular space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 901
ChainResidue
ALYS699
AASP702
AGLU704
AASP707
ATHR824
AGLU825

site_idAC2
Number of Residues6
Detailsbinding site for residue CA B 901
ChainResidue
BASP707
BTHR824
BGLU825
BLYS699
BASP702
BGLU704

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. VDGLDIDiE
ChainResidueDetails
AVAL178-GLU186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000305|PubMed:23865566
ChainResidueDetails
AGLU186
BGLU186

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDS, ECO:0007744|PDB:6MDV
ChainResidueDetails
AARG72
ATRP74
AASP108
AHIS109
ATYR252
AGLU288
AGLU289
AASN295
ATYR339
BARG72
BTRP74
BASP108
BHIS109
BTYR252
BGLU288
BGLU289
BASN295
BTYR339

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDV
ChainResidueDetails
AHIS88
BHIS88

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDS
ChainResidueDetails
AHIS107
AASP184
AGLN250
BHIS107
BASP184
BGLN250

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6E58, ECO:0007744|PDB:6MDS, ECO:0007744|PDB:6MDV
ChainResidueDetails
ALYS699
AASP702
AGLU704
AASP707
ATHR824
AGLU825
BLYS699
BASP702
BGLU704
BASP707
BTHR824
BGLU825

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PDB entries from 2024-05-15

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