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2XHY

Crystal Structure of E.coli BglA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0008706molecular_function6-phospho-beta-glucosidase activity
A0015926molecular_functionglucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0103047molecular_functionmethyl beta-D-glucoside 6-phosphate glucohydrolase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0008706molecular_function6-phospho-beta-glucosidase activity
B0015926molecular_functionglucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0103047molecular_functionmethyl beta-D-glucoside 6-phosphate glucohydrolase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0008706molecular_function6-phospho-beta-glucosidase activity
C0015926molecular_functionglucosidase activity
C0016052biological_processcarbohydrate catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0103047molecular_functionmethyl beta-D-glucoside 6-phosphate glucohydrolase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0008706molecular_function6-phospho-beta-glucosidase activity
D0015926molecular_functionglucosidase activity
D0016052biological_processcarbohydrate catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0103047molecular_functionmethyl beta-D-glucoside 6-phosphate glucohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 1480
ChainResidue
ALYS53

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1481
ChainResidue
AHOH2370
ATRP351
ASER432
APHE433
ATHR434
ALYS440
ATYR442
AHOH2368
AHOH2369

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 1482
ChainResidue
ASER439
AHIS450

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 1483
ChainResidue
AGLY299
ALEU301

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR B 1481
ChainResidue
BARG231

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR B 1482
ChainResidue
BLYS53

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 1483
ChainResidue
BPRO190
BLEU191

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 1484
ChainResidue
BTRP351
BSER432
BPHE433
BTHR434
BLYS440
BTYR442
BHOH2354
BHOH2395
BHOH2396
BHOH2397

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1485
ChainResidue
BLEU247
BSER263
BGLU336
BHOH2398

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 1486
ChainResidue
BGLY299
BASP300
BLEU301
BHOH2281

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 1487
ChainResidue
BASN206
BGLU208
BGLU209
BPHE292

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR C 1480
ChainResidue
CSER439
CHIS450

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR C 1481
ChainResidue
CALA104

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 C 1482
ChainResidue
CTRP351
CSER432
CPHE433
CTHR434
CLYS440
CTYR442
CHOH2431
CHOH2477
CHOH2478
CHOH2479

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR C 1483
ChainResidue
CLYS53
DLYS295

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR D 1480
ChainResidue
DLYS410
DTYR414

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR D 1481
ChainResidue
DGLU336
DHOH2292

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR D 1482
ChainResidue
DSER439
DHIS450
DASP451
DHOH2367

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR D 1483
ChainResidue
DGLN144

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR D 1484
ChainResidue
DPRO190
DLEU191

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR D 1485
ChainResidue
DASN206
DGLU208
DGLU209
DHOH2206

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 1486
ChainResidue
DTRP351
DPHE433
DTHR434
DLYS440
DTYR442
DHOH2398
DHOH2399
DHOH2400

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR D 1487
ChainResidue
DGLY299
DLEU301
DHOH2274

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFIVENGFG
ChainResidueDetails
ALEU373-GLY381

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGgAvAAHQvEgG
ChainResidueDetails
APHE12-GLY26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU180
BGLU180
CGLU180
DGLU180

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU377
BGLU377
CGLU377
DGLU377

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PDB entries from 2024-05-01

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