2j5h

NMR analysis of mouse CRIPTO CFC domain

Method: SOLUTION NMR
▼

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

TERATOCARCINOMA-DERIVED GROWTH FACTOR

OrganismNot specified

UniProt P51865

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TDGF1_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–40; UniProt 96–134

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id2j5h
Deposition date deposition_date2006-09-18
Structure title titleNMR analysis of mouse CRIPTO CFC domain
Keywords keywords;HORMONE/GROWTH FACTOR, GROWTH FACTOR, EGF-CFC FAMILY, CRIPTO, TUMOUR PROGRESSION, CYSTEINE-RICH DOMAINS, HORMONE-GROWTH FACTOR COMPLEX ;; HORMONE/GROWTH FACTOR
Experimental Method methodSOLUTION NMR
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2j5h__assembly_1__model_5

Assembly 1 · Model 5 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2j5h__assembly_1__model_5 | I(q)

10-2 10-1 104 105 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2j5h__assembly_1__model_5 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)11.75 Å
Rg (electron density)10.87 Å
Total Rg12.15 Å
Atom count524
Residues39
Excluded volume5521 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2j5h__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2j5h__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2j5h__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2j5h__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2j5h__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2j5h__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2j5h__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2j5h__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2j5h__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2j5h__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2j5ha1
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.7 — Cripto EGF-like domain-like
▶

7. Citations (1)