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3CMJ

Crystal Structure of engineered Beta-Glucosidase from Soil metagenome

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1
ChainResidue
AGLY60
AHOH489
AHOH570
AHOH579

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 2
ChainResidue
APRO79
AHOH558
AHOH561
AHOH803

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 3
ChainResidue
AHOH819

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 4
ChainResidue
ALYS83
AASN84
AASP86
AGLU444
ATYR446
ASER447

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 5
ChainResidue
ASER87
AHOH512
AHOH734
AHOH792

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 6
ChainResidue
AARG106
AGLY109
AHOH674
AHOH726

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 7
ChainResidue
AASP167
AHOH507
AHOH559

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 8
ChainResidue
AGLN123
AARG128
AGLU182
AHOH491

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 9
ChainResidue
ATYR446
APHE457
AHOH587
AHOH808

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 10
ChainResidue
AGLU143
ALYS147
AHOH809

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 12
ChainResidue
ALEU172
ASER173
AARG174
AARG229
ATYR368

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 13
ChainResidue
AGLU168
ASER173
AGLU175
ASER176
AHOH497

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 14
ChainResidue
AGLN243
AHOH704

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 15
ChainResidue
AALA247
AASP473

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 16
ChainResidue
APHE217
AGLU441
AALA443
AGLU444
AHOH640

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 17
ChainResidue
AILE82
AHOH561

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 483
ChainResidue
AASP393
AGLN406
AHOH839
AHOH848

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 485
ChainResidue
AGLN318
AHOH548
AHOH606
AHOH722

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 486
ChainResidue
ATYR332
ATHR356
ATRP360
AGLY389
AHOH502

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 487
ChainResidue
ATHR356
AMET358
ATRP360
AALA390
AALA391
APHE450

site_idCC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SRT A 488
ChainResidue
AGLN57
AHIS158
AASN202
AGLU203
ATYR332
AGLU387
ATRP434
AGLU441
ATRP442
AHOH672

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAA
ChainResidueDetails
AILE383-ALA391

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGaAtSSYQiEgA
ChainResidueDetails
APHE47-ALA61

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU387
AGLU203
AASN330

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU203
AGLU387

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU203

222036

PDB entries from 2024-07-03

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