Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AYH

CRYSTAL AND MOLECULAR STRUCTURE AT 1.6 ANGSTROMS RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M)

Replaces:  1AYH
Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 417
ChainResidue
APRO9
AGLY45
AASP207
AHOH216
AHOH217
AHOH218

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU105-THR115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU105

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU109

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 924
ChainResidueDetails
AGLU105covalent catalysis
AGLU109proton shuttle (general acid/base)

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon