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3CBW

Crystal structure of the YdhT protein from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0006080biological_processsubstituted mannan metabolic process
A0016985molecular_functionmannan endo-1,4-beta-mannosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0006080biological_processsubstituted mannan metabolic process
B0016985molecular_functionmannan endo-1,4-beta-mannosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT B 1
ChainResidue
AMET117
ASER118
ALYS121
AASN122
BSER215
BLYS218
BGLN219
BLYS222

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CIT B 2
ChainResidue
BHIS370
BHIS368

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CIT B 3
ChainResidue
BHIS369
BHIS370

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P49424
ChainResidueDetails
AGLU193
BGLU193

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P49424
ChainResidueDetails
AGLU292
BGLU292

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P49424
ChainResidueDetails
AHIS131
ATRP198
ATYR268
ATRP324
BHIS131
BTRP198
BTYR268
BTRP324

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Plays an important role in maintaining the position of the catalytic nucleophile => ECO:0000250|UniProtKB:P49424
ChainResidueDetails
AHIS192
BHIS192

222624

PDB entries from 2024-07-17

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