1fmo

CRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED RECOMBINANT CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH THE PEPTIDE INHIBITOR PKI(5-24) AND ADENOSINE

Method: X-RAY DIFFRACTION Dmax: 67.0 Å Quality: GOOD

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

CAMP-DEPENDENT PROTEIN KINASE

Mus musculus

UniProt P05132

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–350 Fragment:CATALYTIC SUBUNIT Non-standard monomer:Yes (specific site not provided by mmCIF) HEAT STABLE RABBIT SKELETAL MUSCLE INHIBITOR PROTEIN × 1 (P61926) ADN ADENOSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;ORTHORHOMBIC CRYSTALS OF THE TERNARY COMPLEX, COMPRISED OF MOUSE HIS6-RC SUBUNIT, PKI (5-24) AND ADENOSINE, WERE GROWN BY THE HANGING-DROP VAPOUR DIFFUSION METHOD USING 2-METHYL-2,4-PENTANEDIOL (MPD) AS THE PRECIPITATING AGENT. THE MOTHER-LIQUOR CONTAINED PROTEIN AT A CONCENTRATION OF 0.25 MM IN 100 MM BICINE BUFFER AT PH 8.0, 0.75 MM PKI(5-24), 4 MM ADENOSINE AND 4% MPD. THE RESERVOIR SOLUTION WAS MADE UP OF 20% MPD IN 100 MM BICINE BUFFER (PH 8.0). X-RAY DIFFRACTION QUALITY CRYSTALS (0.2 X 0.15 X 0.8 MM3) WERE GROWN AT 4 C IN APPROXIMATELY 4 - 6 WEEKS., vapor diffusion - hanging drop, temperature 277K Resolution 2.20 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.

84 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–350; UniProt 1–350

HEAT STABLE RABBIT SKELETAL MUSCLE INHIBITOR PROTEIN

OrganismNot specified

UniProt P61926

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 5–24 Fragment:RESIDUES 5 - 24 CAMP-DEPENDENT PROTEIN KINASE × 1 (P05132) ADN ADENOSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;ORTHORHOMBIC CRYSTALS OF THE TERNARY COMPLEX, COMPRISED OF MOUSE HIS6-RC SUBUNIT, PKI (5-24) AND ADENOSINE, WERE GROWN BY THE HANGING-DROP VAPOUR DIFFUSION METHOD USING 2-METHYL-2,4-PENTANEDIOL (MPD) AS THE PRECIPITATING AGENT. THE MOTHER-LIQUOR CONTAINED PROTEIN AT A CONCENTRATION OF 0.25 MM IN 100 MM BICINE BUFFER AT PH 8.0, 0.75 MM PKI(5-24), 4 MM ADENOSINE AND 4% MPD. THE RESERVOIR SOLUTION WAS MADE UP OF 20% MPD IN 100 MM BICINE BUFFER (PH 8.0). X-RAY DIFFRACTION QUALITY CRYSTALS (0.2 X 0.15 X 0.8 MM3) WERE GROWN AT 4 C IN APPROXIMATELY 4 - 6 WEEKS., vapor diffusion - hanging drop, temperature 277K Resolution 2.20 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPKA_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–20; UniProt 5–24

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 1fmo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fmo
Deposition date deposition_date1997-07-08
Structure title titleCRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED RECOMBINANT CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH THE PEPTIDE INHIBITOR PKI(5-24) AND ADENOSINE
Keywords keywords;COMPLEX (PHOSPHOTRANSFERASE-INHIBITOR), PHOSPHORYLATION, POLYHISTIDINE-TAG, PROTEIN KINASE, COMPLEX (PHOSPHOTRANSFERASE-INHIBITOR) complex ;; COMPLEX (PHOSPHOTRANSFERASE/INHIBITOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.45
Radius of gyration Rg (electron density) rg_electron20.14
Forward intensity I(0) i028372900.00
Molecular weight molecular_weight41983.0 kDa
Excluded volume excluded_volume53009 ų
Envelope volume envelope_volume60485 ų
Hydration-shell volume shell_volume24341 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg27.45
Envelope Rg envelope_rg20.41
Shape Rg shape_rg20.10
Total Rg total_rg21.22
Total atoms total_atoms2968
Residues n_residues356
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 dmax67.0
Rg (real space) rg_real21.31
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.8370e+07
I(0) uncertainty (real space) i0_real_error3.6340e+05
Rg (reciprocal space) rg_reciprocal21.33
I(0) (reciprocal space) i0_reciprocal28370000.0000
Solution quality estimate total_estimate0.8969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.386
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8209000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fmoe_
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 (2 domains)

Domain ID domain_id1fmoE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id1fmoE02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1

8. Citations (6)

9. Files and Curves (10)