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2X09

Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE X09 A 1900
ChainResidue
AILE202
ATRP642
ATRP653
AHOH2437
AASP203
ATRP204
AGLU394
ACYS419
ASER468
AASP469
ATYR516
AGLU541

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE X09 B 1900
ChainResidue
BILE202
BASP203
BTRP204
BGLU394
BCYS419
BSER468
BASP469
BTYR516
BGLU541
BTRP642
BTRP653
BTRP781
BHOH2415
BHOH2708

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1901
ChainResidue
AHIS244
AASP246
AHOH2212

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1902
ChainResidue
AASP296
AHOH2261

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 1901
ChainResidue
BASN428
BGLY429
BGLU431
BGLY433
BHOH2371

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:18976664
ChainResidueDetails
AASP469
BASP469

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:18976664
ChainResidueDetails
AGLU541
BGLU541

226707

PDB entries from 2024-10-30

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