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1UD3

Crystal structure of AmyK38 N289H mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005509molecular_functioncalcium ion binding
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1001
ChainResidue
AASN104
AASP194
AASN200
AHIS235
AHOH2032

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
AASN427
AHOH2182
AGLY300
ATYR302
ATRP403
AASP404

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AGLU261

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AASP328
ATRP263
AGLU261

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AASP328
AARG229
AGLU261
AHIS327

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP231
AGLU261
AHIS105

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP231
AGLU261

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PDB entries from 2025-06-25

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