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

5HNN

Crystal structure of the endo-beta-1,4-glucanase (Xac0030) from Xanthomonas axonopodis pv. citri with the triple mutation His174Trp, Tyr211Ala and Lys227Arg.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
C0000272biological_processpolysaccharide catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
ATYR92
AGLU134
AGLU246
ATRP279
AHOH520
AHOH550

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL B 401
ChainResidue
BTRP279
BHOH501
BHOH504
BHOH507
BHOH511
BTYR92
BGLU134
BGLU246

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL C 401
ChainResidue
CHIS90
CTYR92
CASN133
CGLU134
CTYR206
CGLU246
CTRP279
CHOH516

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VIFGLMNEPN
ChainResidueDetails
AVAL127-ASN136

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon