1MSB
STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HO A 1 |
Chain | Residue |
A | ASP161 |
A | GLU165 |
A | ASP188 |
A | GLU193 |
A | ASP194 |
A | HOH222 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HO A 2 |
Chain | Residue |
A | GLU185 |
A | ASN187 |
A | GLU193 |
A | ASN205 |
A | ASP206 |
A | HOH223 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HO B 1 |
Chain | Residue |
B | HOH31 |
B | ASP161 |
B | GLU165 |
B | ASP188 |
B | GLU193 |
B | ASP194 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HO B 2 |
Chain | Residue |
B | HOH32 |
B | GLU185 |
B | ASN187 |
B | GLU193 |
B | ASN205 |
B | ASP206 |
site_id | HO1 |
Number of Residues | 6 |
Details |
Chain | Residue |
A | ASP161 |
A | GLU165 |
A | ASP188 |
A | GLU193 |
A | ASP194 |
A | HOH222 |
site_id | HO2 |
Number of Residues | 6 |
Details |
Chain | Residue |
A | ASN205 |
A | ASP206 |
A | HOH223 |
A | GLU185 |
A | ASN187 |
A | GLU193 |
site_id | HO3 |
Number of Residues | 6 |
Details |
Chain | Residue |
B | ASP161 |
B | GLU165 |
B | ASP188 |
B | GLU193 |
B | ASP194 |
B | HOH31 |
site_id | HO4 |
Number of Residues | 6 |
Details |
Chain | Residue |
B | GLU185 |
B | ASN187 |
B | GLU193 |
B | ASN205 |
B | ASP206 |
B | HOH32 |
Functional Information from PROSITE/UniProt
site_id | PS00615 |
Number of Residues | 23 |
Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVtivdngl.....WNDISCqasht.AVC |
Chain | Residue | Details |
A | CYS195-CYS217 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532, ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA, ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD, ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ, ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH, ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB |
Chain | Residue | Details |
A | ASP161 | |
A | GLU165 | |
A | ASP188 | |
A | ASP194 | |
B | ASP161 | |
B | GLU165 | |
B | ASP188 | |
B | ASP194 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532, ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB |
Chain | Residue | Details |
A | GLU185 | |
B | ASP206 | |
A | ASN187 | |
A | GLU193 | |
A | ASN205 | |
A | ASP206 | |
B | GLU185 | |
B | ASN187 | |
B | GLU193 | |
B | ASN205 |