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1TML

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030245biological_processcellulose catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 360
ChainResidue
APRO76
ASER85
AGLY77
AARG78
AASP79
ACYS80
AGLY81
AASN82
AHIS83
ASER84

Functional Information from PROSITE/UniProt
site_idPS00655
Number of Residues17
DetailsGLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYnaPgRDCGnhSSgG
ChainResidueDetails
AVAL71-GLY87

site_idPS00656
Number of Residues10
DetailsGLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. YIIVEPDLIS
ChainResidueDetails
ATYR111-SER120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AASP79

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP117

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP265

218853

PDB entries from 2024-04-24

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