5las

HIF prolyl hydroxylase 2 (PHD2-R281C/P317C/R396T) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-3)

Method: X-RAY DIFFRACTION Dmax: 78.9 Å Quality: GOOD

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

Egl nine homolog 1

Homo sapiens

UniProt Q9GZT9

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 181–426 Chain B; UniProt 181–426 Fragment:CATALYTIC DOMAIN, UNP residues 181-426 Mutation:C201A, R281C, P317C, R396T, R398A Hypoxia-inducible factor 1-alpha × 2 (Q16665) 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

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.

63 other PDB entries and 84 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGLN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–252; UniProt 181–426 Author chain B; PDBConstruct 7–252; UniProt 181–426

Hypoxia-inducible factor 1-alpha

OrganismNot specified

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 C; UniProt 395–413 Chain D; UniProt 395–413 Fragment:N-TERMINAL OXYGEN DEPENDENT DEGRADATION DOMAIN (NODD), UNP RESIDUES 395-413; Mutation:L397C, D412C Egl nine homolog 1 × 2 (Q9GZT9) 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

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.

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

View Construct and Data Evidence
UniProt name HIF1A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–19; UniProt 395–413 Author chain D; PDBConstruct 1–19; UniProt 395–413

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.

SAXS scattering curve SAXS Profile

SAXS profile for 5las

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5las
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5las
Deposition date deposition_date2016-06-14
Structure title titleHIF prolyl hydroxylase 2 (PHD2-R281C/P317C/R396T) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-3)
Keywords keywords;OXIDOREDUCTASE, NON-HEME DIOXYGENASE, IRON, 2-OXOGLUTARATE, HYPOXIA-INDUCIBLE FACTOR, HIF, HIF PROLYL HYDROXYLASE DOMAIN 2, PHD2, EGLN1, OXYGENASE, HYPOXIA, DNA-BINDING, METAL-BINDING, TRANSCRIPTION, HELIX-LOOP-HELIX-BETA, DSBH, FACIAL TRIAD, CYTOPLASM, TRANSCRIPTION/EPIGENETIC REGULATION, SIGNALING, DEVELOPMENT, CELL STRUCTURE, BETA-HYDROXYLATION, TRANSCRIPTION ACTIVATOR/INHIBITOR, UBL CONJUGATION, POLYMORPHISM, VITAMIN C, ZINC-FINGER, FAMILIAL ERYTHROCYTOSIS, BREAST CANCER, TRANSCRIPTION COMPLEX ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.27
Radius of gyration Rg (electron density) rg_electron23.67
Forward intensity I(0) i044399700.00
Molecular weight molecular_weight50050.0 kDa
Excluded volume excluded_volume61893 ų
Envelope volume envelope_volume71978 ų
Hydration-shell volume shell_volume25714 ų
Envelope diameter envelope_diameter78.4
Shell Rg shell_rg30.67
Envelope Rg envelope_rg23.95
Shape Rg shape_rg23.65
Total Rg total_rg24.54
Total atoms total_atoms6677
Residues n_residues464
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax78.9
Rg (real space) rg_real24.32
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real4.4400e+07
I(0) uncertainty (real space) i0_real_error6.3330e+05
Rg (reciprocal space) rg_reciprocal24.31
I(0) (reciprocal space) i0_reciprocal44400000.0000
Solution quality estimate total_estimate0.8824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15770000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5lasA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily620 — q2cbj1_9rhob like domain
Domain ID domain_id5lasB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily620 — q2cbj1_9rhob like domain

8. Citations (3)

9. Files and Curves (10)