4AI8
FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH DAMINOZIDE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003714 | molecular_function | transcription corepressor activity |
| A | 0005112 | molecular_function | Notch binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019826 | molecular_function | oxygen sensor activity |
| A | 0031406 | molecular_function | carboxylic acid binding |
| A | 0036139 | molecular_function | peptidyl-histidine dioxygenase activity |
| A | 0036140 | molecular_function | [protein]-asparagine 3-dioxygenase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045663 | biological_process | positive regulation of myoblast differentiation |
| A | 0045746 | biological_process | negative regulation of Notch signaling pathway |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0051059 | molecular_function | NF-kappaB binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0062101 | molecular_function | peptidyl-aspartic acid 3-dioxygenase activity |
| A | 0071532 | molecular_function | ankyrin repeat binding |
| A | 2001214 | biological_process | positive regulation of vasculogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1350 |
| Chain | Residue |
| A | LYS311 |
| A | ALA312 |
| A | HOH2088 |
| A | HOH2119 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1351 |
| Chain | Residue |
| A | PHE224 |
| A | GLU225 |
| A | LYS315 |
| A | HOH2129 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1352 |
| Chain | Residue |
| A | ARG320 |
| A | LYS324 |
| A | HOH2124 |
| A | HOH2135 |
| A | LYS107 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1353 |
| Chain | Residue |
| A | ARG143 |
| A | GLU192 |
| A | GLY193 |
| A | LEU285 |
| A | ASN286 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1354 |
| Chain | Residue |
| A | GLY140 |
| A | GLU141 |
| A | GLU142 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1355 |
| Chain | Residue |
| A | TYR102 |
| A | GLN147 |
| A | THR196 |
| A | HOH2073 |
| A | HOH2076 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1356 |
| Chain | Residue |
| A | LYS99 |
| A | TYR230 |
| A | SER240 |
| A | GLN241 |
| A | ASP243 |
| A | HOH2101 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1357 |
| Chain | Residue |
| A | TYR71 |
| A | LYS75 |
| A | ASN257 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DZA A 1358 |
| Chain | Residue |
| A | TYR145 |
| A | THR196 |
| A | HIS199 |
| A | ASP201 |
| A | ASN205 |
| A | PHE207 |
| A | LYS214 |
| A | HIS279 |
| A | ILE281 |
| A | ASN294 |
| A | ZN1359 |
| A | HOH2073 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1359 |
| Chain | Residue |
| A | HIS199 |
| A | ASP201 |
| A | HIS279 |
| A | DZA1358 |
| A | HOH2073 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:21251231 |
| Chain | Residue | Details |
| A | TYR145 | |
| A | THR196 | |
| A | ASN205 | |
| A | LYS214 | |
| A | ASN294 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21177872 |
| Chain | Residue | Details |
| A | ASP152 | |
| A | GLN181 | |
| A | ARG238 | |
| A | ALA300 | |
| A | ASN321 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794 |
| Chain | Residue | Details |
| A | HIS199 | |
| A | ASP201 | |
| A | HIS279 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Important for dimer formation |
| Chain | Residue | Details |
| A | LEU340 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 |
