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4K35

The structure of a glycoside hydrolase family 81 endo-[beta]-1,3-glucanase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
A0052861molecular_functionendo-1,3(4)-beta-glucanase activity
A0071555biological_processcell wall organization
B0000272biological_processpolysaccharide catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
B0052861molecular_functionendo-1,3(4)-beta-glucanase activity
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 801
ChainResidue
ATYR386
APHE468
AASP475
ATYR478
AHIS479
AGLU557
AHOH1091
AHOH1454

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 802
ChainResidue
AGLU634
ATHR672
AHOH1081
AHOH1094
AASP98

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 801
ChainResidue
BTYR386
BPHE468
BASP475
BTYR478
BHIS479
BGLU557
BTYR628
BHOH954
BHOH1398

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS B 802
ChainResidue
BGLU634
BTHR672
BHOH1119
BHOH1180

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 803
ChainResidue
AILE687
APRO719
BPRO655
BILE687
BHIS720
BHOH1524

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsRegion: {"description":"May provide specificity for triple-helical beta-glucan","evidences":[{"source":"PubMed","id":"34801773","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5XBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5XC2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01352","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34801773","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5XBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5XC2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01352","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01352","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24100321","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"34801773","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4K3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5XBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5XC2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34801773","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5XC2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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