6bz3

Complex structure of FAK FAT domain and DCC P3 motif

Method: X-RAY DIFFRACTION

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

Focal adhesion kinase 1

Mus musculus

UniProt P34152

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Netrin receptor DCC × 2 (Q63155) CALCIUM ION × 1 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FAK1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–126; UniProt 959–1084 Author chain C; PDBConstruct 1–126; UniProt 959–1084

Netrin receptor DCC

OrganismNot specified

UniProt Q63155

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Focal adhesion kinase 1 × 2 (P34152) CALCIUM ION × 1 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DCC_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–23; UniProt 1421–1443 Author chain D; PDBConstruct 1–23; UniProt 1421–1443

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_id6bz3
Deposition date deposition_date2017-12-22
Structure title titleComplex structure of FAK FAT domain and DCC P3 motif
Keywords keywords;4-helix bundle, axon guidance, focal adhesion kinase, transferase-peptide complex, MEMBRANE PROTEIN, TRANSFERASE-MEMBRANE PROTEIN complex ;; TRANSFERASE/MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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.

6bz3__assembly_1__model_1

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

Download this curve (.dat)

6bz3__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6bz3__assembly_1__model_1 | 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)23.40 Å
Rg (electron density)22.76 Å
Total Rg23.54 Å
Atom count2218
Residues287
Excluded volume40314 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6bz3__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (4)

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6bz3A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily330 — Nucleotidyltransferases domain 2
Domain ID domain_id6bz3C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily330 — Nucleotidyltransferases domain 2

7. Citations (1)