2VKH
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF LETHAL TOXIN FROM CLOSTRIDIUM SORDELLII IN COMPLEX WITH UDP-GLC AND CALCIUM ION
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A1543 |
Chain | Residue |
A | ASP288 |
A | GLU515 |
A | SER518 |
A | UPG1544 |
A | HOH2064 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE UPG A1544 |
Chain | Residue |
A | LEU265 |
A | ALA266 |
A | SER269 |
A | ASP270 |
A | ARG273 |
A | TYR284 |
A | ASP286 |
A | VAL287 |
A | ASP288 |
A | ASN384 |
A | GLN385 |
A | THR465 |
A | SER518 |
A | CA1543 |
A | HOH2034 |
A | HOH2064 |
A | ILE101 |
A | TRP102 |
A | ILE103 |
A | ASN139 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B1543 |
Chain | Residue |
B | ASP288 |
B | GLU515 |
B | SER518 |
B | UPG1544 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE UPG B1544 |
Chain | Residue |
B | ILE101 |
B | TRP102 |
B | ILE103 |
B | ASN139 |
B | ALA266 |
B | SER269 |
B | ASP270 |
B | ARG273 |
B | TYR284 |
B | ASP286 |
B | VAL287 |
B | ASP288 |
B | ASN384 |
B | GLN385 |
B | THR465 |
B | GLY470 |
B | SER518 |
B | CA1543 |
B | HOH2031 |
B | HOH2060 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C1543 |
Chain | Residue |
C | ASP288 |
C | GLU515 |
C | SER518 |
C | UPG1544 |
C | HOH2044 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE UPG C1544 |
Chain | Residue |
C | ILE101 |
C | TRP102 |
C | ILE103 |
C | ASN139 |
C | LEU265 |
C | ALA266 |
C | SER269 |
C | ASP270 |
C | ARG273 |
C | TYR284 |
C | ASP286 |
C | VAL287 |
C | ASP288 |
C | ASN384 |
C | GLN385 |
C | THR465 |
C | SER518 |
C | CA1543 |
C | HOH2042 |
C | HOH2044 |
C | HOH2075 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0000269|PubMed:18505687, ECO:0007744|PDB:2VKD, ECO:0007744|PDB:2VKH, ECO:0007744|PDB:2VL8 |
Chain | Residue | Details |
A | ILE101 | |
C | ASN139 | |
C | LEU265 | |
C | ASP286 | |
A | ASN139 | |
A | LEU265 | |
A | ASP286 | |
B | ILE101 | |
B | ASN139 | |
B | LEU265 | |
B | ASP286 | |
C | ILE101 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0007744|PDB:2VKD, ECO:0007744|PDB:2VKH |
Chain | Residue | Details |
A | ASP288 | |
A | GLU515 | |
B | ASP288 | |
B | GLU515 | |
C | ASP288 | |
C | GLU515 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0000269|PubMed:18505687, ECO:0007744|PDB:2VKH, ECO:0007744|PDB:2VL8 |
Chain | Residue | Details |
A | SER518 | |
B | SER518 | |
C | SER518 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P16154 |
Chain | Residue | Details |
A | GLU545 | |
B | GLU545 | |
C | GLU545 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P18177 |
Chain | Residue | Details |
A | ASP546 | |
B | ASP546 | |
C | ASP546 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P18177 |
Chain | Residue | Details |
A | LEU543 | |
B | LEU543 | |
C | LEU543 |