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3ZIZ

Crystal structure of Podospora anserina GH5 beta-(1,4)-mannanase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016985molecular_functionmannan endo-1,4-beta-mannosidase activity
A0046355biological_processmannan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1351
ChainResidue
ATYR27
ATRP56
AASP116
ALYS288
AHOH2024
AHOH2098
AHOH2174
AHOH2223

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 1352
ChainResidue
AGLU169
AGLU276
ATRP308
AHOH2024
AHOH2174
AHOH2196
AHOH2452
AASN168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23558681","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23558681","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B4XC07","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q99036","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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