4BUR
Crystal structure of the reduced human Apoptosis inducing factor complexed with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046983 | molecular_function | protein dimerization activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046983 | molecular_function | protein dimerization activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 700 |
| Chain | Residue |
| A | LEU267 |
| A | ALA397 |
| A | VAL398 |
| A | GLY399 |
| A | GLU453 |
| A | HIS454 |
| A | TRP483 |
| A | FAD1612 |
| A | HOH2006 |
| A | GLY308 |
| A | GLY309 |
| A | PHE310 |
| A | LEU311 |
| A | GLU314 |
| A | PRO335 |
| A | GLU336 |
| A | LYS342 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NAD A 701 |
| Chain | Residue |
| A | TRP196 |
| A | TRP483 |
| A | GLU493 |
| A | PHE582 |
| A | ASN583 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD B 700 |
| Chain | Residue |
| B | LEU267 |
| B | GLY307 |
| B | GLY308 |
| B | GLY309 |
| B | PHE310 |
| B | LEU311 |
| B | GLU314 |
| B | PRO335 |
| B | GLU336 |
| B | LYS342 |
| B | ALA397 |
| B | VAL398 |
| B | GLY399 |
| B | GLU453 |
| B | HIS454 |
| B | TRP483 |
| B | FAD1612 |
| B | HOH2004 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NAD B 701 |
| Chain | Residue |
| B | TRP196 |
| B | TRP483 |
| B | GLU493 |
| B | PHE582 |
| B | ASN583 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD C 700 |
| Chain | Residue |
| C | LEU267 |
| C | GLY308 |
| C | GLY309 |
| C | PHE310 |
| C | LEU311 |
| C | GLU314 |
| C | PRO335 |
| C | GLU336 |
| C | LYS342 |
| C | ALA397 |
| C | VAL398 |
| C | GLY399 |
| C | GLU453 |
| C | HIS454 |
| C | TRP483 |
| C | FAD1612 |
| C | HOH2003 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NAD C 701 |
| Chain | Residue |
| A | ALA275 |
| C | TRP196 |
| C | TRP483 |
| C | GLU493 |
| C | PHE582 |
| C | ASN583 |
| C | HOH2007 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD D 700 |
| Chain | Residue |
| D | LEU267 |
| D | GLY307 |
| D | GLY308 |
| D | GLY309 |
| D | PHE310 |
| D | LEU311 |
| D | GLU314 |
| D | PRO335 |
| D | GLU336 |
| D | ALA397 |
| D | VAL398 |
| D | GLY399 |
| D | GLU453 |
| D | HIS454 |
| D | TRP483 |
| D | FAD1612 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NAD D 701 |
| Chain | Residue |
| D | TRP196 |
| D | ASP456 |
| D | MET481 |
| D | TRP483 |
| D | GLU493 |
| D | PHE582 |
| D | ASN583 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 1612 |
| Chain | Residue |
| A | ARG172 |
| A | PRO173 |
| A | SER176 |
| A | LYS177 |
| A | VAL233 |
| A | ALA259 |
| A | THR260 |
| A | GLY261 |
| A | ARG285 |
| A | GLY437 |
| A | ASP438 |
| A | GLU453 |
| A | HIS454 |
| A | HIS455 |
| A | ALA458 |
| A | PHE482 |
| A | TRP483 |
| A | NAD700 |
| A | HOH2001 |
| A | HOH2002 |
| A | HOH2004 |
| A | GLY138 |
| A | GLY139 |
| A | GLY140 |
| A | THR141 |
| A | ALA142 |
| A | VAL162 |
| A | GLU164 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 1612 |
| Chain | Residue |
| B | GLY138 |
| B | GLY139 |
| B | GLY140 |
| B | THR141 |
| B | ALA142 |
| B | VAL162 |
| B | GLU164 |
| B | ARG172 |
| B | PRO173 |
| B | SER176 |
| B | LYS231 |
| B | LYS232 |
| B | VAL233 |
| B | ALA259 |
| B | THR260 |
| B | GLY261 |
| B | PHE284 |
| B | ARG285 |
| B | GLY437 |
| B | ASP438 |
| B | GLU453 |
| B | HIS454 |
| B | HIS455 |
| B | ALA458 |
| B | PHE482 |
| B | NAD700 |
| site_id | BC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD D 1612 |
| Chain | Residue |
| D | GLY138 |
| D | GLY139 |
| D | GLY140 |
| D | THR141 |
| D | ALA142 |
| D | VAL162 |
| D | GLU164 |
| D | ARG172 |
| D | PRO173 |
| D | SER176 |
| D | LYS177 |
| D | LYS232 |
| D | VAL233 |
| D | ALA259 |
| D | THR260 |
| D | GLY261 |
| D | ARG285 |
| D | GLY437 |
| D | ASP438 |
| D | GLU453 |
| D | HIS454 |
| D | HIS455 |
| D | ALA458 |
| D | PHE482 |
| D | NAD700 |
| site_id | BC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD C 1612 |
| Chain | Residue |
| C | GLY138 |
| C | GLY139 |
| C | GLY140 |
| C | THR141 |
| C | ALA142 |
| C | VAL162 |
| C | GLU164 |
| C | ARG172 |
| C | PRO173 |
| C | SER176 |
| C | LYS177 |
| C | LYS231 |
| C | LYS232 |
| C | VAL233 |
| C | ALA259 |
| C | THR260 |
| C | GLY261 |
| C | ARG285 |
| C | GLY437 |
| C | ASP438 |
| C | GLU453 |
| C | HIS454 |
| C | HIS455 |
| C | ALA458 |
| C | PHE482 |
| C | TRP483 |
| C | NAD700 |
| C | HOH2001 |
| C | HOH2002 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1613 |
| Chain | Residue |
| B | ARG584 |
| D | ASN583 |
| D | ARG584 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6, ECO:0007744|PDB:5FS7, ECO:0007744|PDB:5FS8, ECO:0007744|PDB:5FS9, ECO:0007744|PDB:5KVI |
| Chain | Residue | Details |
| A | GLY138 | |
| B | GLY138 | |
| C | GLY138 | |
| D | GLY138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6, ECO:0007744|PDB:5FS7, ECO:0007744|PDB:5FS8, ECO:0007744|PDB:5FS9, ECO:0007744|PDB:5KVH, ECO:0007744|PDB:5KVI |
| Chain | Residue | Details |
| A | GLU164 | |
| C | ARG172 | |
| C | VAL233 | |
| C | ASP438 | |
| D | GLU164 | |
| D | ARG172 | |
| D | VAL233 | |
| D | ASP438 | |
| A | ARG172 | |
| A | VAL233 | |
| A | ASP438 | |
| B | GLU164 | |
| B | ARG172 | |
| B | VAL233 | |
| B | ASP438 | |
| C | GLU164 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6, ECO:0007744|PDB:5FS7, ECO:0007744|PDB:5FS8, ECO:0007744|PDB:5FS9, ECO:0007744|PDB:5KVI |
| Chain | Residue | Details |
| A | LYS177 | |
| B | LYS177 | |
| C | LYS177 | |
| D | LYS177 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24914854, ECO:0007744|PDB:4BUR |
| Chain | Residue | Details |
| A | TRP196 | |
| B | GLU336 | |
| B | GLY399 | |
| B | GLU453 | |
| B | GLU493 | |
| B | ASN583 | |
| C | TRP196 | |
| C | GLY308 | |
| C | GLU336 | |
| C | GLY399 | |
| C | GLU453 | |
| A | GLY308 | |
| C | GLU493 | |
| C | ASN583 | |
| D | TRP196 | |
| D | GLY308 | |
| D | GLU336 | |
| D | GLY399 | |
| D | GLU453 | |
| D | GLU493 | |
| D | ASN583 | |
| A | GLU336 | |
| A | GLY399 | |
| A | GLU453 | |
| A | GLU493 | |
| A | ASN583 | |
| B | TRP196 | |
| B | GLY308 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6, ECO:0007744|PDB:5FS7, ECO:0007744|PDB:5FS8, ECO:0007744|PDB:5FS9, ECO:0007744|PDB:5KVH |
| Chain | Residue | Details |
| A | ARG285 | |
| B | ARG285 | |
| C | ARG285 | |
| D | ARG285 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Z0X1 |
| Chain | Residue | Details |
| A | LYS342 | |
| B | LYS342 | |
| C | LYS342 | |
| D | LYS342 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6, ECO:0007744|PDB:5FS7, ECO:0007744|PDB:5FS8, ECO:0007744|PDB:5FS9, ECO:0007744|PDB:5KVH, ECO:0007744|PDB:5KVI |
| Chain | Residue | Details |
| A | HIS454 | |
| B | HIS454 | |
| C | HIS454 | |
| D | HIS454 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24914854, ECO:0007744|PDB:4BUR, ECO:0007744|PDB:4BV6 |
| Chain | Residue | Details |
| A | TRP483 | |
| B | TRP483 | |
| C | TRP483 | |
| D | TRP483 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR105 | |
| B | THR105 | |
| C | THR105 | |
| D | THR105 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z0X1 |
| Chain | Residue | Details |
| A | LYS109 | |
| B | LYS109 | |
| C | LYS109 | |
| D | LYS109 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER116 | |
| B | SER116 | |
| C | SER116 | |
| D | SER116 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER118 | |
| C | SER371 | |
| C | SER524 | |
| C | SER530 | |
| D | SER118 | |
| D | SER371 | |
| D | SER524 | |
| D | SER530 | |
| A | SER371 | |
| A | SER524 | |
| A | SER530 | |
| B | SER118 | |
| B | SER371 | |
| B | SER524 | |
| B | SER530 | |
| C | SER118 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER268 | |
| B | SER268 | |
| C | SER268 | |
| D | SER268 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER292 | |
| B | SER292 | |
| C | SER292 | |
| D | SER292 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z0X1 |
| Chain | Residue | Details |
| A | LYS388 | |
| A | LYS593 | |
| B | LYS388 | |
| B | LYS593 | |
| C | LYS388 | |
| C | LYS593 | |
| D | LYS388 | |
| D | LYS593 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR521 | |
| B | THR521 | |
| C | THR521 | |
| D | THR521 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22103349 |
| Chain | Residue | Details |
| A | LYS255 | |
| B | LYS255 | |
| C | LYS255 | |
| D | LYS255 |
