SAXSdb — 1h2m

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1. Protein Identity and Related Structures Protein Identity & Related Structures

FACTOR INHIBITING HIF1

HOMO SAPIENS

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–349	Not recorded	HYPOXIA-INDUCIBLE FACTOR 1 ALPHA × 2 （Q16665） ZN ZINC ION × 2 OGA N-OXALYLGLYCINE × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, 11MG/ML PROTEIN WITH 1MM ZN(II), 2.5MM NOG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.50 Å R-free 0.225

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1H2M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H2K Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide Deposited 2002-08-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–349（349 aa）	Not recorded	FE2 FE (II) ION × 2 OGA N-OXALYLGLYCINE × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM FE(II), 2.5MM NOG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.15 Å R-free 0.213
1H2L Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide Deposited 2002-08-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–349（349 aa）	Not recorded	FE2 FE (II) ION × 2 AKG 2-OXOGLUTARIC ACID × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM FE(II), 2.5MM AKG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.25 Å R-free 0.217

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q969Q7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–349； UniProt 1–349

HYPOXIA-INDUCIBLE FACTOR 1 ALPHA

HOMO SAPIENS

UniProt Q16665

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain S； UniProt 775–826	Fragment：C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES 775-826	FACTOR INHIBITING HIF1 × 2 （Q969Q7） ZN ZINC ION × 2 OGA N-OXALYLGLYCINE × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, 11MG/ML PROTEIN WITH 1MM ZN(II), 2.5MM NOG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.50 Å R-free 0.225

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1H2M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H2K Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide Deposited 2002-08-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain S 786–826（41 aa） Fragment：C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES 786-826	Not recorded	FE2 FE (II) ION × 2 OGA N-OXALYLGLYCINE × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM FE(II), 2.5MM NOG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.15 Å R-free 0.213
1H2L Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide Deposited 2002-08-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain S 786–826（41 aa） Fragment：C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES 786-826	Not recorded	FE2 FE (II) ION × 2 AKG 2-OXOGLUTARIC ACID × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM FE(II), 2.5MM AKG AND 2.5MM PEPTIDE, pH 7.50	Resolution 2.25 Å R-free 0.217
1L3E NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex Deposited 2002-02-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 785–826（42 aa） Fragment：C-terminal transactivation domain (CTAD)	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure ambient NMR sample composition 1mM CTAD/CH1 complex U-15N,13C; 0.1mM ZnSO4; 1mM DTT \| 90% D2O, 10% H2O NMR sample composition 1mM CTAD/CH1 complex U-15N,13C; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O NMR sample composition 1mM CTAD/CH1 complex U-15N; 0.1mM ZnSO4; 1mM DTT \| 90% D2O, 10% H2O NMR sample composition 1mM CTAD/CH1 complex; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O NMR sample composition 1mM CTAD/CH1 complex 10% U-13C; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O	Resolution not provided
1L8C STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THE CELLULAR HYPOXIC RESPONSE Deposited 2002-03-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 776–826（51 aa） Fragment：CTAD (C-Terminal activation) domain, Residues 776-826	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.1；298 K；Ionic strength (raw mmCIF value) 2.0 Millimolar；Pressure Ambient NMR sample composition 1MM 13C, 15N-TAZ1, 2MM HIF-1a NMR sample composition 1MM 13C, 15N-HIF-1a, 2MM TAZ1 NMR sample composition 10MM D-TRIS, 10MM D-DTT, 0.02% NAN3, 0.5MM ZnSO4	Resolution not provided
1LM8 Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex Deposited 2002-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 556–575（20 aa） Fragment：Residues 556-575	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.85 Å R-free 0.236
1LQB Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex Deposited 2002-05-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 549–582（34 aa） Fragment：residues 549-582	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；HEPES, PEG2000 monomethylester, ammonium sulfate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.00 Å R-free 0.277
1LQB Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex Deposited 2002-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain D 549–582（34 aa） Fragment：residues 549-582	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；HEPES, PEG2000 monomethylester, ammonium sulfate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.00 Å R-free 0.277
2ILM Factor Inhibiting HIF-1 Alpha D201A Mutant in Complex with FE(II), Alpha-Ketoglutarate and HIF-1 Alpha 35mer Deposited 2006-10-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain S 786–826（41 aa） Fragment：CTAD	Not recorded	FE2 FE (II) ION × 2 SO4 SULFATE ION × 4 BCT BICARBONATE ION × 2 AKG 2-OXOGLUTARIC ACID × 2 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；1.6M AMMONIUM SULPHATE, 6% PEG400, 0.1M HEPES PH7.5 ARGON ATMOSPHERE, 14MG/ML PROTEIN WITH 1MM FE(II)SO4, 1MM ALPHA-KETOGLUTARATE, 1MM HIF-1ALPHA PEPTIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K, pH 7.50	Resolution 2.30 Å R-free 0.267
3HQR PHD2:Mn:NOG:HIF1-alpha substrate complex Deposited 2009-06-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 558–574（17 aa） Fragment：C-terminal degradation domain, residues 558-574	Not recorded	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 7.5；298 K；20% PEG 3350, 200mM MgCl2, pH 7.5, hanging drop, temperature 298K	Resolution 2.00 Å R-free 0.248
3HQU PHD2:Fe:UN9:partial HIF1-alpha substrate complex Deposited 2009-06-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 558–574（17 aa） Fragment：C-terminal degradation domain, residues 558-574	Not recorded	FE2 FE (II) ION × 1 UN9 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 6.5；298 K；1.6M AMMONIUM SULFATE, 4% DIOXANE, 0.1M MES PH6.5, ARGON ATMOSPHERE, 20MG/ML PROTEIN WITH 1MM FE(II)SO4, 10MM HIF1A-CODD-OH PEPTIDE, hanging drop, temperature 298K	Resolution 2.30 Å R-free 0.222
4AJY von Hippel-Lindau protein-ElonginB-ElonginC complex, bound to Hif1- alpha peptide Deposited 2012-02-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 559–577（19 aa） Fragment：RESIDUES 559-577	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 0.1 M K PHOSPHATE PH 6.6 0.2 M (NH4)2SO4 20% PEG MME 5000 5 MM DTT	Resolution 1.73 Å R-free 0.232
4H6J Identification of Cys 255 in HIF-1 as a novel site for development of covalent inhibitors of HIF-1 /ARNT PasB domain protein-protein interaction. Deposited 2012-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 238–348（111 aa） Fragment：PAS-B DOMAIN, UNP residues 238-348	Mutation：R245E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；20% PEG 8000, 0.2M MgCl2, 0.1M Tris pH 8.5 , VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.52 Å R-free 0.248
5JWP Crystal structure of human FIH D201E variant in complex with Zn, alpha-ketoglutarate, and HIF1 alpha peptide. Deposited 2016-05-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 788–806（19 aa） Fragment：UNP residues 11-29	Not recorded	AKG 2-OXOGLUTARIC ACID × 2 GOL GLYCEROL × 2 ZN ZINC ION × 2 SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Hepes, 1.6mM ammonium sulfate, 3% PEG 400	Resolution 2.10 Å R-free 0.209
5L9B HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) IN COMPLEX WITH 2-OXOGLUTARATE (2OG) AND HIF-1ALPHA CODD (556-574) Deposited 2016-06-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 556–574（19 aa） Fragment：UNP residues 556-574	Not recorded	MN MANGANESE (II) ION × 1 AKG 2-OXOGLUTARIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Magnesium chloride hexahydrate, 0.1 M BIS-TRIS pH 5.5, 25% w/v polyethylene glycol 3350	Resolution 1.95 Å R-free 0.186
5L9B HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) IN COMPLEX WITH 2-OXOGLUTARATE (2OG) AND HIF-1ALPHA CODD (556-574) Deposited 2016-06-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 556–574（19 aa） Fragment：UNP residues 556-574	Not recorded	MN MANGANESE (II) ION × 1 AKG 2-OXOGLUTARIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Magnesium chloride hexahydrate, 0.1 M BIS-TRIS pH 5.5, 25% w/v polyethylene glycol 3350	Resolution 1.95 Å R-free 0.186
5L9V HIF prolyl hydroxylase 2 (PHD2-R281C/P317C) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-1) Deposited 2016-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP RESIDUES 395-413	Mutation：L397C, D412C	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.2 M ammonium chloride, 20 % w/v polyethylene glycol 3350	Resolution 1.83 Å R-free 0.190
5L9V HIF prolyl hydroxylase 2 (PHD2-R281C/P317C) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-1) Deposited 2016-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP RESIDUES 395-413	Mutation：L397C, D412C	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.2 M ammonium chloride, 20 % w/v polyethylene glycol 3350	Resolution 1.83 Å R-free 0.190
5LA9 HIF prolyl hydroxylase 2 (PHD2-R281C/V314C) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-2) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP residues 395-413	Mutation：L397C, D412C	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M HEPES pH 7.5, 2.0 M ammonium sulfate	Resolution 2.81 Å R-free 0.279
5LA9 HIF prolyl hydroxylase 2 (PHD2-R281C/V314C) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-2) Deposited 2016-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP residues 395-413	Mutation：L397C, D412C	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M HEPES pH 7.5, 2.0 M ammonium sulfate	Resolution 2.81 Å R-free 0.279
5LAS HIF prolyl hydroxylase 2 (PHD2-R281C/P317C/R396T) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-3) Deposited 2016-06-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP RESIDUES 395-413; Chain D 395–413（19 aa） Fragment：N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP RESIDUES 395-413;	Mutation：L397C, D412C Mutation：L397C, D412C	MN MANGANESE (II) ION × 2 OGA N-OXALYLGLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；0.1 M citrate pH 5.0, 20 % w/v polyethylene glycol 6000	Resolution 2.10 Å R-free 0.221
6YW3 HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) in complex with N-Oxalyl Glycine (NOG), HIF-1ALPHA CODD (556-574) and a RaPID-derived cyclic peptide 3C (14-mer) Deposited 2020-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain S 556–574（19 aa）	Not recorded	MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；Sample: 1.0 mM cPHD2, 1.5 mM MnCl2, 2.0 mM compound, 1.0 mM 3C, 2.0 mM CODD; Reservoir: 19-23% w/v polyethylene glycol 3350, 0.25 M lithium sulfate, 2 mM MnCl2; Sitting drop (2 ul), protein-to-well ratio, 1:1	Resolution 2.28 Å R-free 0.208
7LVS The CBP TAZ1 Domain in Complex with a CITED2-HIF-1-Alpha Fusion Peptide Deposited 2021-02-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 796–826（31 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 6.87, 28% PEG 4000	Resolution 2.02 Å R-free 0.241
7QGS Crystal structure of p300 CH1 domain in complex with CITIF (a CITED2-HIF-1alpha hybrid) Deposited 2021-12-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 792–826（35 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M HEPES pH 6.5, PEG 6K 35%	Resolution 2.00 Å R-free 0.245
8HE0 Crystal structure of importin-alpha1 bound to the HIF-1alpha nuclear localization signal (wild-type) Deposited 2022-11-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 717–757（41 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；293 K；tri-sodium citrate, HEPES, DTT	Resolution 1.80 Å R-free 0.198
9OFU Dimer of HIF-1a-ARNT Heterodimers Complexed on 52-bp HRE/HAS Deposited 2025-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain A 3–361（359 aa） Chain C 3–361（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；50mM HEPES, 150mM NaCl, 5mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HIFA_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain S； PDBConstruct 1–52； UniProt 775–826

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h2m
Deposition date deposition_date	2002-08-12
Structure title title	Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide
Keywords keywords	;TRANSCRIPTION ACTIVATOR-INHIBITOR COMPLEX, FIH, HIF, DSBH, OXYGENASE, TRANSCRIPTION, HYPOXIA, 2- OXOGLUTARATE, ASPARAGINYL HYDROXYLASE, HYDROXYLASE ;; TRANSCRIPTION ACTIVATOR/INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	21.55 Å
Radius of gyration Rg (electron density) rg_electron	20.36 Å
Forward intensity I(0) i0	28826300.00
Molecular weight molecular_weight	40817.0 kDa
Excluded volume excluded_volume	50812 Å³
Envelope volume envelope_volume	60687 Å³
Hydration-shell volume shell_volume	24254 Å³
Envelope diameter envelope_diameter	72.3 Å
Shell Rg shell_rg	27.69 Å
Envelope Rg envelope_rg	20.83 Å
Shape Rg shape_rg	20.33 Å
Total Rg total_rg	21.40 Å
Total atoms total_atoms	2880
Residues n_residues	354
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	70.5 Å
Rg (real space) rg_real	21.43 Å
Rg uncertainty (real space) rg_real_error	0.35 Å
I(0) (real space) i0_real	2.8830e+07
I(0) uncertainty (real space) i0_real_error	3.5520e+05
Rg (reciprocal space) rg_reciprocal	21.45 Å
I(0) (reciprocal space) i0_reciprocal	28830000.0000
Solution quality estimate total_estimate	0.8778
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.0 Å
Skewness Skewness skewness	0.236
Kurtosis Kurtosis kurtosis	-0.246
Angular range angular_range	— – 0.3700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6784000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.985

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	FACTOR INHIBITING HIF1
Molecular weight formula_weight	40328.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2979

MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	HYPOXIA-INDUCIBLE FACTOR 1 ALPHA
Molecular weight formula_weight	5662.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S

PSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	N-OXALYLGLYCINE
Molecular weight formula_weight	147.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	99

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1h2ma_
Class class	b — All beta proteins
Fold Fold fold	b.82 — Double-stranded beta-helix
Superfamily Superfamily superfamily	b.82.2 — Clavaminate synthase-like
Family Family family	b.82.2.6 — Hypoxia-inducible factor HIF ihhibitor (FIH1)

CATH v4.4 (2 domains)

Domain ID domain_id	1h2mA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	10 — Jelly Rolls

Domain ID domain_id	1h2mA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	1010 — Clavaminate synthase-like

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8. Citations (1)

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Unit-cell length a length_a	86.249 Å
Unit-cell length b length_b	86.249 Å
Unit-cell length c length_c	148.260 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	18.000 Å
R factor r_factor	0.1940
R_work r_work	0.1920
R_free r_free	0.2250

fit	/app/data/saxs_computation/h2/1h2m/1h2m.fit
pddf	/app/data/pr_computation/h2/1h2m/1h2m.pr.out
profile	/app/data/saxs_computation/h2/1h2m/1h2m.dat

Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide

1. Protein Identity and Related Structures Protein Identity & Related Structures

FACTOR INHIBITING HIF1

State in the Current Structure

Other States of the Same Protein in the Database

HYPOXIA-INDUCIBLE FACTOR 1 ALPHA

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)