Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1J0I

Crystal structure of neopullulanase complex with panose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005509molecular_functioncalcium ion binding
A0005536molecular_functionD-glucose binding
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031216molecular_functionneopullulanase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005509molecular_functioncalcium ion binding
B0005536molecular_functionD-glucose binding
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031216molecular_functionneopullulanase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J0H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU357

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BGLU357
BASP424

site_idCSA11
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AHIS423
AASP328
AARG326
AGLU357
AASP424

site_idCSA12
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BHIS423
BASP328
BARG326
BGLU357
BASP424

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BGLU357

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
ATRP359
AGLU357
AASP424

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BTRP359
BGLU357
BASP424

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP208
AASP269

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP208
BASP269

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU357
AHIS247
AASP424

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BGLU357
BHIS247
BASP424

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU357
AASP424

243531

PDB entries from 2025-10-22

PDB statisticsPDBj update infoContact PDBjnumon