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1JF6

Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031216molecular_functionneopullulanase activity
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031216molecular_functionneopullulanase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AASN143
AASP145
AASN148
AASP149
AGLY169
AASP171

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 602
ChainResidue
BASP149
BGLY169
BASP171
BASN143
BASP145
BASN148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AASP325
BASP325

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AGLU354
BGLU354

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2
ChainResidueDetails
AASN143
BASP149
BGLY169
BASP171
AASP145
AASN148
AASP149
AGLY169
AASP171
BASN143
BASP145
BASN148

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AHIS244
BARG469
AARG323
AHIS420
AASP465
AARG469
BHIS244
BARG323
BHIS420
BASP465

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP421
BASP421

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP325
ALEU350

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP325
BGLU354

site_idCSA11
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP325
AASP421
AARG323
AGLU354
AHIS420

site_idCSA12
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP325
BASP421
BARG323
BGLU354
BHIS420

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP325
BLEU350

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
ATRP356
AASP325
AASP421
AGLU354

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BTRP356
BASP325
BASP421
BGLU354

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP421
AASP325
AGLU354
AHIS244

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP421
BASP325
BGLU354
BHIS244

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP421
AASP325
AGLU354

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP421
BASP325
BGLU354

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP325
AGLU354

site_idMCSA1
Number of Residues3
DetailsM-CSA 433
ChainResidueDetails
AASP325covalent catalysis
AGLU354proton shuttle (general acid/base)
AASP421transition state stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 433
ChainResidueDetails
BASP325covalent catalysis
BGLU354proton shuttle (general acid/base)
BASP421transition state stabiliser

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PDB entries from 2024-10-30

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