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4DM2

Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase

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 Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AGLY221
AMET222
AASN258
APRO259

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 501
ChainResidue
BHOH698
BTRP272
BTRP273
BVAL303
BGOL503
BHOH631

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BASP302
BLYS346
BGLY350
BGLY351
BASP352
BASP385

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
BTYR299
BTRP377
BASP385
BGOL501
BGOL504
BGOL505

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 504
ChainResidue
ATHR213
AASP214
BPHE69
BGLU72
BARG156
BTRP377
BGOL503
BGOL505
BHOH628
BHOH629
BHOH703

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 505
ChainResidue
AALA210
ATHR213
AASP214
BGLY384
BASP385
BGOL503
BGOL504

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. IGADLKNEPH
ChainResidueDetails
AILE194-HIS203

223166

PDB entries from 2024-07-31

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