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 |
