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HUMAN GLYCOSYLATION-INHIBITING FACTOR

Method: X-RAY DIFFRACTION Dmax: 59.0 Å Quality: GOOD

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

GLYCOSYLATION-INHIBITING 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 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å

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

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gif
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gif
Deposition date deposition_date1996-02-27
Structure title titleHUMAN GLYCOSYLATION-INHIBITING FACTOR
Keywords keywordsMACROPHAGE, INFLAMMATORY RESPONSE, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.01
Radius of gyration Rg (electron density) rg_electron18.78
Forward intensity I(0) i024151200.00
Molecular weight molecular_weight37432.0 kDa
Excluded volume excluded_volume46723 ų
Envelope volume envelope_volume51969 ų
Hydration-shell volume shell_volume22363 ų
Envelope diameter envelope_diameter56.7
Shell Rg shell_rg25.89
Envelope Rg envelope_rg18.78
Shape Rg shape_rg18.79
Total Rg total_rg19.64
Total atoms total_atoms2625
Residues n_residues345
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 dmax59.0
Rg (real space) rg_real19.84
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real2.4150e+07
I(0) uncertainty (real space) i0_real_error2.6630e+05
Rg (reciprocal space) rg_reciprocal19.87
I(0) (reciprocal space) i0_reciprocal24150000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.003
Kurtosis Kurtosis kurtosis-0.555
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4867000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1gifa_
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_idd1gifb_
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_idd1gifc_
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_id1gifA00
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_id1gifB00
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_id1gifC00
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)