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5Z0T

Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE)

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
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
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 701
ChainResidue
AALA2
AASP4
AASN6
AASP42
AASP96
AHOH1003

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 702
ChainResidue
AASP151
AGLY187
AASP189
AHOH826
AASN145
AASP147
AASN150

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 703
ChainResidue
AASP276
AASN279
APHE281
ASER283
AGLU288
AHOH1369

site_idAC4
Number of Residues6
Detailsbinding site for residue MPD A 704
ChainResidue
AHIS221
ATYR223
APHE313
AHOH945
AHOH1061
AHOH1377

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 701
ChainResidue
BALA2
BASP4
BASN6
BASP42
BASP96
BHOH935

site_idAC6
Number of Residues7
Detailsbinding site for residue CA B 702
ChainResidue
BASN145
BASP147
BASN150
BASP151
BGLY187
BASP189
BHOH833

site_idAC7
Number of Residues6
Detailsbinding site for residue CA B 703
ChainResidue
BASP276
BASN279
BPHE281
BSER283
BGLU288
BHOH1460

site_idAC8
Number of Residues5
Detailsbinding site for residue MPD B 704
ChainResidue
BHIS221
BTYR223
BPHE313
BHOH839
BHOH877

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AASP356
BASP356

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AGLU396
BGLU396

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1
ChainResidueDetails
AALA2
AGLY187
AASP189
AASP276
AASN280
APHE281
ASER283
AGLU288
BALA2
BASP4
BASN6
AASP4
BASP42
BASP96
BASN145
BASP147
BASN150
BASP151
BGLY187
BASP189
BASP276
BASN280
AASN6
BPHE281
BSER283
BGLU288
AASP42
AASP96
AASN145
AASP147
AASN150
AASP151

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P38940
ChainResidueDetails
AHIS267
BARG520
AARG354
AHIS471
AASP516
AARG520
BHIS267
BARG354
BHIS471
BASP516

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP472
BASP472

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PDB entries from 2024-09-04

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