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5DUY

Structure of lectin from the sea mussel Crenomytilus grayanus

Functional Information from GO Data
ChainGOidnamespacecontents
A0030246molecular_functioncarbohydrate binding
B0030246molecular_functioncarbohydrate binding
C0030246molecular_functioncarbohydrate binding
D0030246molecular_functioncarbohydrate binding
E0030246molecular_functioncarbohydrate binding
F0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue GOL A 201
ChainResidue
AHIS16
AASN119
APRO17
ATYR18
AGLY19
AGLY20
AVAL31
AHIS33
AASP35
AHIS37

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 202
ChainResidue
AASN27
AHIS64
AGLY67
AGLY68
AHIS81
AASP83
AHIS85

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 203
ChainResidue
AGLU75
AHIS108
APRO109
ALYS110
AGLY111
AGLY112
AVAL123
AHIS125
AHIS129
AHOH330

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL B 201
ChainResidue
BHIS16
BGLY19
BGLY20
BHIS33
BASP35
BHIS37
BASN119

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 202
ChainResidue
BASN27
BHIS64
BGLY67
BGLY68
BHIS81
BASP83
BHIS85
BHOH334

site_idAC6
Number of Residues10
Detailsbinding site for residue GOL B 203
ChainResidue
BGLU75
BHIS108
BPRO109
BLYS110
BGLY111
BGLY112
BVAL123
BHIS125
BHIS129
BHOH333

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL C 201
ChainResidue
CHIS16
CGLY19
CGLY20
CHIS33
CASP35
CHIS37
CASN119

site_idAC8
Number of Residues10
Detailsbinding site for residue GOL C 202
ChainResidue
BHOH304
BHOH320
CASN27
CHIS64
CTYR66
CGLY67
CGLY68
CHIS81
CHIS85
CHOH302

site_idAC9
Number of Residues9
Detailsbinding site for residue GOL C 203
ChainResidue
CGLU75
CHIS108
CPRO109
CLYS110
CGLY111
CGLY112
CVAL123
CHIS125
CHIS129

site_idAD1
Number of Residues10
Detailsbinding site for residue GOL D 201
ChainResidue
ATYR18
AHOH302
DHIS16
DPRO17
DGLY19
DGLY20
DHIS33
DASP35
DHIS37
DASN119

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL D 202
ChainResidue
DASN27
DHIS64
DGLY67
DGLY68
DASP83
DHIS85

site_idAD3
Number of Residues9
Detailsbinding site for residue GOL D 203
ChainResidue
DGLY112
DHIS125
DHIS129
DHOH332
DGLU75
DHIS108
DPRO109
DLYS110
DGLY111

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL E 201
ChainResidue
EHIS16
EPRO17
EGLY19
EGLY20
EASP35
EHIS37
EASN119

site_idAD5
Number of Residues7
Detailsbinding site for residue GOL E 202
ChainResidue
AHOH304
EASN27
EHIS64
EGLY67
EGLY68
EHIS81
EHIS85

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL E 203
ChainResidue
EGLU75
EHIS108
ELYS110
EGLY111
EGLY112
EHIS125
EHIS129

site_idAD7
Number of Residues8
Detailsbinding site for residue GOL F 201
ChainResidue
FHIS16
FPRO17
FGLY19
FGLY20
FHIS33
FASP35
FHIS37
FASN119

site_idAD8
Number of Residues10
Detailsbinding site for residue GOL F 202
ChainResidue
EHOH302
EHOH353
FASN27
FHIS64
FTYR66
FGLY67
FGLY68
FHIS81
FASP83
FHIS85

site_idAD9
Number of Residues8
Detailsbinding site for residue GOL F 203
ChainResidue
FGLU75
FHIS108
FPRO109
FLYS110
FGLY111
FGLY112
FHIS125
FHIS129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27010847","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F8W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27010847","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F90","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"5F8W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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