6RLC
Crystal structure of the PDZ tandem of syntenin in complex with fragment F13
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0007268 | biological_process | chemical synaptic transmission |
A | 0030036 | biological_process | actin cytoskeleton organization |
A | 0035556 | biological_process | intracellular signal transduction |
B | 0007268 | biological_process | chemical synaptic transmission |
B | 0030036 | biological_process | actin cytoskeleton organization |
B | 0035556 | biological_process | intracellular signal transduction |
C | 0007268 | biological_process | chemical synaptic transmission |
C | 0030036 | biological_process | actin cytoskeleton organization |
C | 0035556 | biological_process | intracellular signal transduction |
D | 0007268 | biological_process | chemical synaptic transmission |
D | 0030036 | biological_process | actin cytoskeleton organization |
D | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue K7Z A 301 |
Chain | Residue |
A | HIS208 |
A | LEU258 |
D | SER259 |
D | THR260 |
D | SER261 |
D | HOH419 |
A | VAL209 |
A | GLY210 |
A | PHE211 |
A | ILE212 |
A | PHE213 |
A | ASP251 |
A | SER252 |
A | ALA255 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue ACT A 302 |
Chain | Residue |
A | ILE125 |
A | LEU127 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue K7Z B 301 |
Chain | Residue |
B | HIS208 |
B | VAL209 |
B | GLY210 |
B | PHE211 |
B | ILE212 |
B | PHE213 |
B | SER252 |
B | ALA255 |
B | LEU258 |
B | HOH403 |
B | HOH412 |
C | LYS203 |
C | SER259 |
C | THR260 |
C | SER261 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ACT B 302 |
Chain | Residue |
B | ILE125 |
B | GLY126 |
B | LEU127 |
B | ARG128 |
B | LYS179 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue K7Z C 301 |
Chain | Residue |
B | SER259 |
B | THR260 |
B | SER261 |
B | HOH428 |
C | HIS208 |
C | VAL209 |
C | GLY210 |
C | PHE211 |
C | ILE212 |
C | PHE213 |
C | ASP251 |
C | SER252 |
C | ALA255 |
C | LEU258 |
C | HOH410 |
C | HOH412 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for residue K7Z D 301 |
Chain | Residue |
A | LYS203 |
A | SER259 |
A | THR260 |
A | SER261 |
D | HIS208 |
D | VAL209 |
D | GLY210 |
D | PHE211 |
D | ILE212 |
D | PHE213 |
D | ASP251 |
D | SER252 |
D | ALA255 |
D | LEU258 |
D | HOH403 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ACT D 302 |
Chain | Residue |
D | LYS124 |
D | ILE125 |
D | GLY126 |
D | LEU127 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. LqINGENCAGWS |
Chain | Residue | Details |
A | LEU159-SER170 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27386966, ECO:0007744|PDB:4Z33 |
Chain | Residue | Details |
A | ASN215 | |
A | LYS250 | |
B | ASN215 | |
B | LYS250 | |
C | ASN215 | |
C | LYS250 | |
D | ASN215 | |
D | LYS250 |