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1ESL

INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS

Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 163
ChainResidue
AASP106
AHOH249
AHOH315
AGLU80
AASN82
AASN105

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 164
ChainResidue
ATYR3
AASN4
AGLU33
AGLU36
AHOH229
AHOH302

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 165
ChainResidue
AGLN20
ATYR23
AHOH219
AHOH221
AHOH286
AHOH309
AHOH310

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 180
ChainResidue
ATRP1
ASER40
AALA121
AASN138
AASN139
AHOH233

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 181
ChainResidue
ACYS127
ATYR140
AHOH274

site_idS1
Number of Residues6
DetailsCALCIUM IONS LOCATED IN THIS SITE IS BELIEVED TO BE PART OF THE NATIVE STRUCTURE. THE OTHER TWO CALCIUM IONS PROBABLY ARE PRESENT ONLY AS A RESULT OF THE HIGH CALCIUM CONCENTRATION (0.2M) USED IN CRYSTALLIZATION
ChainResidue
AGLU80
AASN82
AASN105
AASP106
AHOH249
AHOH315

Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CkCdpGfsGLkC
ChainResidueDetails
ACYS142-CYS153

site_idPS00615
Number of Residues28
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CVeiyikrekdvgmWNDERCskkkl.ALC
ChainResidueDetails
ACYS90-CYS117

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CkCdpGFsglk....C
ChainResidueDetails
ACYS142-CYS153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsDomain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EGF-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26117840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CSY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26117840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ESL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4C16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CSY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11081633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26117840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ESL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1G1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4C16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CSY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11081633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26117840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CSY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26117840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CSY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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