2ooh

Crystal Structure of MIF bound to a Novel Inhibitor, OXIM-11

Method: X-RAY DIFFRACTION Dmax: 57.9 Å Quality: GOOD

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

Macrophage migration inhibitory factor

Homo sapiens

UniProt P14174

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–114 Chain B; UniProt 1–114 Chain C; UniProt 1–114 Not recorded SO4 SULFATE ION × 8 OX3 4-HYDROXYBENZALDEHYDE O-(CYCLOHEXYLCARBONYL)OXIME × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;296 K;50% saturated ammonium sulfate, 4% isopropanol, 0.1 M tris(hydroxymethyl)aminomethane,mixed with protein:inhibitor complex in a 1:1 ratio, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.85 Å R-free 0.218

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.

117 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MIF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–114; UniProt 1–114 Author chain B; PDBConstruct 1–114; UniProt 1–114 Author chain C; PDBConstruct 1–114; UniProt 1–114

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 2ooh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ooh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ooh
Deposition date deposition_date2007-01-25
Structure title titleCrystal Structure of MIF bound to a Novel Inhibitor, OXIM-11
Keywords keywordsalternative ligand-binding modes, ISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.15
Radius of gyration Rg (electron density) rg_electron18.77
Forward intensity I(0) i025946200.00
Molecular weight molecular_weight38076.0 kDa
Excluded volume excluded_volume47132 ų
Envelope volume envelope_volume52547 ų
Hydration-shell volume shell_volume22520 ų
Envelope diameter envelope_diameter58.2
Shell Rg shell_rg25.95
Envelope Rg envelope_rg18.86
Shape Rg shape_rg18.76
Total Rg total_rg19.67
Total atoms total_atoms2662
Residues n_residues342
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 dmax57.9
Rg (real space) rg_real19.98
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real2.5950e+07
I(0) uncertainty (real space) i0_real_error2.9730e+05
Rg (reciprocal space) rg_reciprocal20.01
I(0) (reciprocal space) i0_reciprocal25950000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.007
Kurtosis Kurtosis kurtosis-0.561
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4851000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2ooha_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.80 — Tautomerase/MIF
Superfamily Superfamily superfamilyd.80.1 — Tautomerase/MIF
Family Family familyd.80.1.3 — MIF-related
Domain ID domain_idd2oohb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.80 — Tautomerase/MIF
Superfamily Superfamily superfamilyd.80.1 — Tautomerase/MIF
Family Family familyd.80.1.3 — MIF-related
Domain ID domain_idd2oohc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.80 — Tautomerase/MIF
Superfamily Superfamily superfamilyd.80.1 — Tautomerase/MIF
Family Family familyd.80.1.3 — MIF-related

CATH v4.4 (3 domains)

Domain ID domain_id2oohA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology429 — Macrophage Migration Inhibitory Factor
Homologous superfamily homologous superfamily10 — Macrophage Migration Inhibitory Factor
Domain ID domain_id2oohB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology429 — Macrophage Migration Inhibitory Factor
Homologous superfamily homologous superfamily10 — Macrophage Migration Inhibitory Factor
Domain ID domain_id2oohC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology429 — Macrophage Migration Inhibitory Factor
Homologous superfamily homologous superfamily10 — Macrophage Migration Inhibitory Factor

8. Citations (1)

9. Files and Curves (10)