8QNS
Crystal structure of murine AIF bound to N-terminal domain of CHCHD4
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046983 | molecular_function | protein dimerization activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046983 | molecular_function | protein dimerization activity |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0046983 | molecular_function | protein dimerization activity |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0046983 | molecular_function | protein dimerization activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11967568, ECO:0000269|PubMed:19447115, ECO:0007744|PDB:3GD3, ECO:0007744|PDB:3GD4 |
Chain | Residue | Details |
A | GLY137 | |
G | ARG171 | |
G | VAL232 | |
G | ARG284 | |
J | GLY137 | |
J | ARG171 | |
J | VAL232 | |
J | ARG284 | |
A | ARG171 | |
A | VAL232 | |
A | ARG284 | |
D | GLY137 | |
D | ARG171 | |
D | VAL232 | |
D | ARG284 | |
G | GLY137 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11967568, ECO:0000269|PubMed:19447115, ECO:0007744|PDB:3GD4 |
Chain | Residue | Details |
A | GLU163 | |
A | HIS453 | |
D | GLU163 | |
D | HIS453 | |
G | GLU163 | |
G | HIS453 | |
J | GLU163 | |
J | HIS453 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11967568, ECO:0000269|PubMed:19447115, ECO:0007744|PDB:3GD3 |
Chain | Residue | Details |
A | LYS176 | |
D | LYS176 | |
G | LYS176 | |
J | LYS176 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O95831 |
Chain | Residue | Details |
A | TRP195 | |
J | TRP195 | |
J | GLU492 | |
J | ASN582 | |
A | GLU492 | |
A | ASN582 | |
D | TRP195 | |
D | GLU492 | |
D | ASN582 | |
G | TRP195 | |
G | GLU492 | |
G | ASN582 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19447115, ECO:0007744|PDB:3GD4 |
Chain | Residue | Details |
A | GLY307 | |
D | GLY398 | |
D | GLU452 | |
D | TRP482 | |
G | GLY307 | |
G | GLU335 | |
G | LYS341 | |
G | GLY398 | |
G | GLU452 | |
G | TRP482 | |
J | GLY307 | |
A | GLU335 | |
J | GLU335 | |
J | LYS341 | |
J | GLY398 | |
J | GLU452 | |
J | TRP482 | |
A | LYS341 | |
A | GLY398 | |
A | GLU452 | |
A | TRP482 | |
D | GLY307 | |
D | GLU335 | |
D | LYS341 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19447115, ECO:0007744|PDB:3GD3, ECO:0007744|PDB:3GD4 |
Chain | Residue | Details |
A | ASP437 | |
D | ASP437 | |
G | ASP437 | |
J | ASP437 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS108 | |
D | LYS108 | |
G | LYS108 | |
J | LYS108 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O95831 |
Chain | Residue | Details |
A | SER115 | |
D | SER529 | |
G | SER115 | |
G | SER267 | |
G | SER370 | |
G | SER523 | |
G | SER529 | |
J | SER115 | |
J | SER267 | |
J | SER370 | |
J | SER523 | |
A | SER267 | |
J | SER529 | |
A | SER370 | |
A | SER523 | |
A | SER529 | |
D | SER115 | |
D | SER267 | |
D | SER370 | |
D | SER523 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
Chain | Residue | Details |
A | LYS387 | |
A | LYS592 | |
D | LYS387 | |
D | LYS592 | |
G | LYS387 | |
G | LYS592 | |
J | LYS387 | |
J | LYS592 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O95831 |
Chain | Residue | Details |
A | THR520 | |
D | THR520 | |
G | THR520 | |
J | THR520 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:O95831 |
Chain | Residue | Details |
A | LYS254 | |
D | LYS254 | |
G | LYS254 | |
J | LYS254 |