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_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 163 |
Chain | Residue |
A | ASP106 |
A | HOH249 |
A | HOH315 |
A | GLU80 |
A | ASN82 |
A | ASN105 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 164 |
Chain | Residue |
A | TYR3 |
A | ASN4 |
A | GLU33 |
A | GLU36 |
A | HOH229 |
A | HOH302 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 165 |
Chain | Residue |
A | GLN20 |
A | TYR23 |
A | HOH219 |
A | HOH221 |
A | HOH286 |
A | HOH309 |
A | HOH310 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 180 |
Chain | Residue |
A | TRP1 |
A | SER40 |
A | ALA121 |
A | ASN138 |
A | ASN139 |
A | HOH233 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 181 |
Chain | Residue |
A | CYS127 |
A | TYR140 |
A | HOH274 |
site_id | S1 |
Number of Residues | 6 |
Details | CALCIUM 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 |
Chain | Residue |
A | GLU80 |
A | ASN82 |
A | ASN105 |
A | ASP106 |
A | HOH249 |
A | HOH315 |
Functional Information from PROSITE/UniProt
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CkCdpGfsGLkC |
Chain | Residue | Details |
A | CYS142-CYS153 |
site_id | PS00615 |
Number of Residues | 28 |
Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVeiyikrekdvgmWNDERCskkkl.ALC |
Chain | Residue | Details |
A | CYS90-CYS117 |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. CkCdpGFsglk....C |
Chain | Residue | Details |
A | CYS142-CYS153 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY |
Chain | Residue | Details |
A | GLU80 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY |
Chain | Residue | Details |
A | ASN82 | |
A | ASN105 | |
A | ASP106 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:26117840, ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY |
Chain | Residue | Details |
A | GLU88 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26117840, ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY |
Chain | Residue | Details |
A | GLU92 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26117840, ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY |
Chain | Residue | Details |
A | ASN4 | |
A | ASN124 | |
A | ASN139 | |
A | ASN158 |