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5OKB

High resolution structure of native Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus

Replaces:  4ZEH
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
A0033920molecular_function6-phospho-beta-galactosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033920molecular_function6-phospho-beta-galactosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0016052biological_processcarbohydrate catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033920molecular_function6-phospho-beta-galactosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0016052biological_processcarbohydrate catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033920molecular_function6-phospho-beta-galactosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue IMD A 501
ChainResidue
AMET262
ATRP285
AGLN289

site_idAC2
Number of Residues4
Detailsbinding site for residue IMD A 502
ChainResidue
AGLY323
AASN349
AGLU383
APHE384

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 503
ChainResidue
AHOH607
AGLU383
APHE384

site_idAC4
Number of Residues4
Detailsbinding site for residue IMD A 504
ChainResidue
AILE173
ATYR301
APO4505
AHOH657

site_idAC5
Number of Residues8
Detailsbinding site for residue PO4 A 505
ChainResidue
AGLN23
ATRP425
ALEU430
ATRP433
ATYR441
AIMD504
AHOH610
AHOH645

site_idAC6
Number of Residues4
Detailsbinding site for residue IMD B 501
ChainResidue
BTRP260
BMET262
BHOH612
DGLN371

site_idAC7
Number of Residues5
Detailsbinding site for residue IMD B 502
ChainResidue
BPRO343
BHIS344
BVAL345
BASP346
CARG157

site_idAC8
Number of Residues10
Detailsbinding site for residue PO4 B 503
ChainResidue
BTRP352
BSER432
BASN435
BLYS439
BTYR441
BHOH634
BHOH638
BHOH665
BHOH899
BHOH962

site_idAC9
Number of Residues3
Detailsbinding site for residue IMD C 501
ChainResidue
CLYS189
CASP190
CHOH1056

site_idAD1
Number of Residues6
Detailsbinding site for residue IMD C 502
ChainResidue
CILE173
CTYR301
CGLU378
CPO4503
CHOH658
CHOH705

site_idAD2
Number of Residues10
Detailsbinding site for residue PO4 C 503
ChainResidue
CGLN23
CTRP425
CLEU430
CSER432
CTRP433
CTYR441
CIMD502
CHOH619
CHOH657
CHOH665

site_idAD3
Number of Residues3
Detailsbinding site for residue IMD D 501
ChainResidue
DLYS189
DASP190
DHOH1007

site_idAD4
Number of Residues3
Detailsbinding site for residue GOL D 502
ChainResidue
DSER176
DALA226
DHOH712

site_idAD5
Number of Residues8
Detailsbinding site for residue PO4 D 503
ChainResidue
DGLN23
DTRP425
DLEU430
DSER432
DTRP433
DTYR441
DHOH637
DHOH659

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. ILITENGLG
ChainResidueDetails
AILE374-GLY382

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGaAsAAYQvEgA
ChainResidueDetails
APHE13-ALA27

221051

PDB entries from 2024-06-12

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