4gum

Cystal structure of locked-trimer of human MIF

Method: X-RAY DIFFRACTION Dmax: 114.6 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 2–115 Chain B; UniProt 2–115 Chain C; UniProt 2–115 Mutation:N110C CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;293 K;0.2M LiSO4, 3% DMSO, pH8.0, 33% PEG4000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.33 Å R-free 0.272
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 2–115 Chain E; UniProt 2–115 Chain F; UniProt 2–115 Mutation:N110C CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;293 K;0.2M LiSO4, 3% DMSO, pH8.0, 33% PEG4000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.33 Å R-free 0.272
3 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 2–115 Chain H; UniProt 2–115 Chain I; UniProt 2–115 Mutation:N110C CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;293 K;0.2M LiSO4, 3% DMSO, pH8.0, 33% PEG4000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.33 Å R-free 0.272

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 130 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 2–115 Author chain B; PDBConstruct 1–114; UniProt 2–115 Author chain C; PDBConstruct 1–114; UniProt 2–115 Author chain D; PDBConstruct 1–114; UniProt 2–115 Author chain E; PDBConstruct 1–114; UniProt 2–115 Author chain F; PDBConstruct 1–114; UniProt 2–115 Author chain G; PDBConstruct 1–114; UniProt 2–115 Author chain H; PDBConstruct 1–114; UniProt 2–115 Author chain I; PDBConstruct 1–114; UniProt 2–115

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 4gum

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gum
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gum
Deposition date deposition_date2012-08-29
Structure title titleCystal structure of locked-trimer of human MIF
Keywords keywordsalpha/beta mixture, cytokine and isomerase, isomerase; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.85
Radius of gyration Rg (electron density) rg_electron35.29
Forward intensity I(0) i0177797000.00
Molecular weight molecular_weight105560.0 kDa
Excluded volume excluded_volume131330 ų
Envelope volume envelope_volume176660 ų
Hydration-shell volume shell_volume42117 ų
Envelope diameter envelope_diameter119.0
Shell Rg shell_rg41.32
Envelope Rg envelope_rg34.82
Shape Rg shape_rg35.27
Total Rg total_rg35.76
Total atoms total_atoms7395
Residues n_residues993
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 dmax114.6
Rg (real space) rg_real35.81
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.7780e+08
I(0) uncertainty (real space) i0_real_error2.9580e+06
Rg (reciprocal space) rg_reciprocal35.84
I(0) (reciprocal space) i0_reciprocal177800000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.733
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47410000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (9 domains)

Domain ID domain_idd4guma_
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_idd4gumb_
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_idd4gumc_
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_idd4gumd_
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_idd4gume_
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_idd4gumf_
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_idd4gumg_
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_idd4gumh_
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_idd4gumi_
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 (9 domains)

Domain ID domain_id4gumA00
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_id4gumB00
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_id4gumC00
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_id4gumD00
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_id4gumE00
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_id4gumF00
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_id4gumG00
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_id4gumH00
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_id4gumI00
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)