1fmk

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC

Method: X-RAY DIFFRACTION Dmax: 78.9 Å Quality: EXCELLENT

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

TYROSINE-PROTEIN KINASE SRC

Homo sapiens

UniProt P12931

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 85–535 Fragment:RESIDUES 86-836, CONTAINING SH2, SH3, KINASE 2 DOMAINS AND C-TERMINAL TAIL Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.50 Å R-free 0.264

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.

76 other PDB entries and 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–452; UniProt 85–535

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 1fmk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fmk
Deposition date deposition_date1997-01-24
Structure title titleCRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Keywords keywordsSRC, TYROSINE KINASE, PHOSPHORYLATION, SH2, SH3, PHOSPHOTYROSINE, PROTO-ONCOGENE, PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.17
Radius of gyration Rg (electron density) rg_electron24.12
Forward intensity I(0) i041992800.00
Molecular weight molecular_weight49981.0 kDa
Excluded volume excluded_volume62581 ų
Envelope volume envelope_volume77580 ų
Hydration-shell volume shell_volume26994 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg31.18
Envelope Rg envelope_rg24.04
Shape Rg shape_rg24.12
Total Rg total_rg24.96
Total atoms total_atoms3516
Residues n_residues437
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 dmax78.9
Rg (real space) rg_real25.10
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.1990e+07
I(0) uncertainty (real space) i0_real_error6.0540e+05
Rg (reciprocal space) rg_reciprocal25.13
I(0) (reciprocal space) i0_reciprocal41990000.0000
Solution quality estimate total_estimate0.9095
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11890000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1fmka1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain
Domain ID domain_idd1fmka2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain
Domain ID domain_idd1fmka3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id1fmkA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1fmkA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1fmkA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id1fmkA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)