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6NCW

Crystal structure of a GH2 beta-galacturonidase from Eisenbergiella tayi bound to glycerol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004566molecular_functionbeta-glucuronidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004566molecular_functionbeta-glucuronidase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004566molecular_functionbeta-glucuronidase activity
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004566molecular_functionbeta-glucuronidase activity
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 601
ChainResidue
ATRP482
AASN531
ALYS532

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 602
ChainResidue
AHOH701
AHOH706
AHOH730
AARG337
AGLU378
ATYR430
ATYR434
AARG525
AGOL603

site_idAC3
Number of Residues11
Detailsbinding site for residue GOL A 603
ChainResidue
AASP131
AHIS312
AARG337
AASN377
AGLU378
AASN428
AGLU465
ATRP510
AGOL602
AHOH701
AHOH752

site_idAC4
Number of Residues3
Detailsbinding site for residue CL B 601
ChainResidue
BTRP482
BASN531
BLYS532

site_idAC5
Number of Residues10
Detailsbinding site for residue GOL B 602
ChainResidue
BASP131
BHIS312
BARG337
BASN377
BGLU378
BASN428
BGLU465
BTRP510
BGOL603
BHOH762

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL B 603
ChainResidue
BARG337
BGLU378
BTYR430
BTYR434
BARG525
BGOL602
BHOH708
BHOH753

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL B 604
ChainResidue
BHIS156
BLYS169
BGLU171
BTYR365
BTYR403
BHOH733
BHOH737

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 605
ChainResidue
BPHE157
BPRO159
BVAL251
BGLY252
BARG254
BASN366
BARG404

site_idAC9
Number of Residues3
Detailsbinding site for residue CL C 601
ChainResidue
CTRP482
CASN531
CLYS532

site_idAD1
Number of Residues10
Detailsbinding site for residue GOL C 602
ChainResidue
CASP131
CHIS312
CARG337
CASN377
CGLU378
CASN428
CGLU465
CTRP510
CGOL603
CHOH835

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL C 603
ChainResidue
CARG337
CGLU378
CTYR430
CTYR434
CARG525
CGOL602
CHOH714
CHOH829

site_idAD3
Number of Residues3
Detailsbinding site for residue CL D 601
ChainResidue
DTRP482
DASN531
DLYS532

site_idAD4
Number of Residues10
Detailsbinding site for residue GOL D 602
ChainResidue
DASP131
DHIS312
DARG337
DASN377
DGLU378
DASN428
DGLU465
DTRP510
DGOL603
DHOH820

site_idAD5
Number of Residues8
Detailsbinding site for residue GOL D 603
ChainResidue
DHOH857
DARG337
DGLU378
DTYR430
DTYR434
DARG525
DGOL602
DHOH729

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PDB entries from 2024-07-10

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