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2E8Y

Crystal structure of pullulanase type I from Bacillus subtilis str. 168

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051060molecular_functionpullulanase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0051060molecular_functionpullulanase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 741
ChainResidue
AASP275
APHE276
AGLU281
AGLU301
AHOH769
AHOH779
AHOH858

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 751
ChainResidue
AARG546
APHE572
AARG595
APHE599
AHOH1057
ATRP530
AASP542

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 742
ChainResidue
BASP275
BPHE276
BGLU281
BGLU301
BHOH813
BHOH828
BHOH874

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 752
ChainResidue
BTRP530
BASP542
BARG546
BPHE572
BARG595
BPHE599

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 761
ChainResidue
AARG223
AGLY237
ALYS238
APRO284
ALEU285
ASER303
AHOH821

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 762
ChainResidue
BPHE69
BGLY70
BLYS71
BHIS73
BLEU85
BGLN86
BILE87
BTHR125
BHOH915

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP406
BASP406

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU435
BGLU435

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP525
BASP525

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP406
AASP525
AGLU435
ATRP437

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP525
BASP406
BGLU435
BHIS340

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP406
BASP525
BGLU435
BTRP437

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP525
AASP406
AGLU435

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP525
BASP406
BGLU435

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP406
AGLU435

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP406
BGLU435

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP406
AASP525
AGLU435
AARG404
AHIS524

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP406
BASP525
BGLU435
BARG404
BHIS524

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP525
AASP406
AGLU435
AHIS340

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PDB entries from 2024-07-17

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