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2D0H

Crystal Structure of Thermoactinomyces vulgaris R-47 Alpha-Amylase 1 (TVAI) Mutant D356N/E396Q complexed with P2, a pullulan model oligosaccharide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031216molecular_functionneopullulanase activity
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AASN356

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AGLN396

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1
ChainResidueDetails
AALA2
AGLY187
AASP189
AASP276
AASN280
APHE281
ASER283
AGLU288
AASP4
AASN6
AASP42
AASP96
AASN145
AASP147
AASN150
AASP151

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AHIS267
AARG354
AHIS471
AASP516
AARG520

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP472

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASN356
AASN435
AGLN396

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASN356
AASP472
AGLN396
ATRP398

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASN356
AGLN396

226707

PDB entries from 2024-10-30

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