3OD4
Crystal Structure of Factor Inhibiting HIF-1 Alpha Complexed with Inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| 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 | 0009966 | biological_process | regulation of signal transduction |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019826 | molecular_function | oxygen sensor activity |
| A | 0030947 | biological_process | regulation of vascular endothelial growth factor receptor signaling pathway |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0050793 | biological_process | regulation of developmental process |
| A | 0051059 | molecular_function | NF-kappaB binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1350 |
| Chain | Residue |
| A | HIS199 |
| A | ASP201 |
| A | HIS279 |
| A | 8XQ350 |
| A | HOH490 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 8XQ A 350 |
| Chain | Residue |
| A | ASP201 |
| A | PHE207 |
| A | LYS214 |
| A | HIS279 |
| A | ILE281 |
| A | ASN294 |
| A | TRP296 |
| A | ZN1350 |
| A | TYR145 |
| A | LEU188 |
| A | THR196 |
| A | HIS199 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 351 |
| Chain | Residue |
| A | ARG138 |
| A | GLY140 |
| A | GLU141 |
| A | GLU142 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 352 |
| Chain | Residue |
| A | LYS107 |
| A | ARG320 |
| A | LYS324 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 353 |
| Chain | Residue |
| A | ARG143 |
| A | GLU192 |
| A | GLY193 |
| A | LEU285 |
| A | ASN286 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 354 |
| Chain | Residue |
| A | LEU150 |
| A | ASN151 |
| A | PHE162 |
| A | HOH496 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 355 |
| Chain | Residue |
| A | ASP201 |
| A | GLN203 |
| A | HOH433 |
| A | HOH435 |
| A | HOH490 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 356 |
| Chain | Residue |
| A | TYR230 |
| A | SER240 |
| A | GLN241 |
| A | HOH376 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 357 |
| Chain | Residue |
| A | GLN148 |
| A | ASN151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 170 |
| Details | Domain: {"description":"JmjC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12432100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12446723","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21251231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21177872","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12432100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12446723","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15913349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17135241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20396966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20822901","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21251231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21460794","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for dimer formation"} |
| Chain | Residue | Details |
