3b9s

Macrophage Migration Inhibitory Factor (MIF) complexed with Inhibitor, 4-IPP.

Method: X-RAY DIFFRACTION Dmax: 60.6 Å Quality: EXCELLENT

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 Not recorded GOL GLYCEROL × 3 RW1 4-phenylpyrimidine × 3 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;2M ammonium sulfate, 4% isopropanol, 0.1 M tris(hydroxymethyl)aminomethan; mixed with protein:inhibitor complex in a 1:10 ratio, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.230

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 2–115 Author chain B; PDBConstruct 1–114; UniProt 2–115 Author chain C; 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 3b9s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3b9s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3b9s
Deposition date deposition_date2007-11-06
Structure title titleMacrophage Migration Inhibitory Factor (MIF) complexed with Inhibitor, 4-IPP.
Keywords keywordsmacrophage migration inhibitory factor, cytokine; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.37
Radius of gyration Rg (electron density) rg_electron18.93
Forward intensity I(0) i025730300.00
Molecular weight molecular_weight38123.0 kDa
Excluded volume excluded_volume47365 ų
Envelope volume envelope_volume53764 ų
Hydration-shell volume shell_volume22841 ų
Envelope diameter envelope_diameter60.3
Shell Rg shell_rg26.18
Envelope Rg envelope_rg19.06
Shape Rg shape_rg18.90
Total Rg total_rg19.91
Total atoms total_atoms2672
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 dmax60.6
Rg (real space) rg_real20.20
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.5730e+07
I(0) uncertainty (real space) i0_real_error3.0850e+05
Rg (reciprocal space) rg_reciprocal20.23
I(0) (reciprocal space) i0_reciprocal25730000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.028
Kurtosis Kurtosis kurtosis-0.538
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5308000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.997

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_idd3b9sa_
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_idd3b9sb_
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_idd3b9sc_
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_id3b9sA00
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_id3b9sB00
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_id3b9sC00
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)