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

5TF0

Crystal Structure of Glycosil Hydrolase Family 3 N-Terminal Domain Protein from Bacteroides intestinalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009251biological_processglucan catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 800
ChainResidue
AASP701
AVAL703
AHOH905
AHOH958
AHOH959
AHOH1030

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 801
ChainResidue
AHIS619
BASN228
APRO614
ALEU615
APHE616

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 802
ChainResidue
AASP112
APHE156
AMSE257
AMSE323
AHOH950

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 803
ChainResidue
AGLY86
AVAL87
AGLU88
AASP150

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 800
ChainResidue
BASP701
BVAL703
BHOH910
BHOH918
BHOH971
BHOH1010

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 801
ChainResidue
BASP112
BMSE257
BASP292
BHOH903
BHOH914
BHOH991

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO B 802
ChainResidue
BGLU99
BSER101
BARG102

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRkQwgfdGFVVTDftG
ChainResidueDetails
AVAL278-GLY295

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon