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1J9Y

Crystal structure of mannanase 26A from Pseudomonas cellulosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005976biological_processpolysaccharide metabolic process
A0006080biological_processsubstituted mannan metabolic process
A0010391biological_processglucomannan metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016985molecular_functionmannan endo-1,4-beta-mannosidase activity
A0051069biological_processgalactomannan metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS71
AGLU239
AHOH1109
AHOH1278
AHOH1335
AHOH1413

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
AHOH1203
AHOH1225
AHOH1347
AASP222
AHOH1123
AHOH1199

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1003
ChainResidue
AHIS79
AASP111
AGLU121
AHOH1542

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1004
ChainResidue
AARG208
AHIS211
AASP283
AGLU320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8973192","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8973192","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Plays an important role in maintaining the position of the catalytic nucleophile","evidences":[{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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