6H9J
Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (229-255)
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 | 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 | 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 | 14 |
Details | binding site for residue OGA A 401 |
Chain | Residue |
A | TYR145 |
A | ASN294 |
A | TRP296 |
A | ZN409 |
A | HOH509 |
A | HOH590 |
A | THR196 |
A | HIS199 |
A | ASP201 |
A | ASN205 |
A | PHE207 |
A | LYS214 |
A | HIS279 |
A | ILE281 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | TYR230 |
A | SER240 |
A | GLN241 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | GLU59 |
A | MET275 |
A | ALA300 |
A | HIS313 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ARG33 |
A | HIS98 |
A | ARG143 |
A | LEU285 |
A | SO4408 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 405 |
Chain | Residue |
A | ARG138 |
A | GLY140 |
A | GLU141 |
A | GLU142 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 406 |
Chain | Residue |
A | LYS311 |
A | ALA312 |
A | HOH514 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | ARG120 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 408 |
Chain | Residue |
A | ARG143 |
A | GLU192 |
A | GLY193 |
A | LEU285 |
A | ASN286 |
A | GOL404 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue ZN A 409 |
Chain | Residue |
A | HIS199 |
A | ASP201 |
A | HIS279 |
A | OGA401 |
A | HOH509 |
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 |