1crk

MITOCHONDRIAL CREATINE KINASE

Method: X-RAY DIFFRACTION D_max: 146.1 Å Quality: GOOD

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

CREATINE KINASE

OrganismNot specified

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 40–419 Chain B； UniProt 40–419 Chain C； UniProt 40–419 Chain D； UniProt 40–419	Not recorded	PO4 PHOSPHATE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.7；pH 6.7	Resolution 3.00 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	KCRS_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–380； UniProt 40–419 Author chain B； PDBConstruct 1–380； UniProt 40–419 Author chain C； PDBConstruct 1–380； UniProt 40–419 Author chain D； PDBConstruct 1–380； UniProt 40–419

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1crk
Deposition date deposition_date	1996-03-08
Structure title title	MITOCHONDRIAL CREATINE KINASE
Keywords keywords	TRANSFERASE, CREATINE KINASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	45.45 Å
Radius of gyration Rg (electron density) rg_electron	45.19 Å
Forward intensity I(0) i0	464029000.00
Molecular weight molecular_weight	173540.0 kDa
Excluded volume excluded_volume	215560 Å³
Envelope volume envelope_volume	296260 Å³
Hydration-shell volume shell_volume	54416 Å³
Envelope diameter envelope_diameter	143.2 Å
Shell Rg shell_rg	50.48 Å
Envelope Rg envelope_rg	43.86 Å
Shape Rg shape_rg	45.20 Å
Total Rg total_rg	45.38 Å
Total atoms total_atoms	12184
Residues n_residues	1520
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	146.1 Å
Rg (real space) rg_real	45.32 Å
Rg uncertainty (real space) rg_real_error	1.19 Å
I(0) (real space) i0_real	4.6400e+08
I(0) uncertainty (real space) i0_real_error	8.5360e+06
Rg (reciprocal space) rg_reciprocal	45.45 Å
I(0) (reciprocal space) i0_reciprocal	464100000.0000
Solution quality estimate total_estimate	0.8041
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	66.8 Å
Skewness Skewness skewness	0.077
Kurtosis Kurtosis kurtosis	-0.644
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	57810000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1crka1
Class class	a — All alpha proteins
Fold Fold fold	a.83 — Guanido kinase N-terminal domain
Superfamily Superfamily superfamily	a.83.1 — Guanido kinase N-terminal domain
Family Family family	a.83.1.1 — Guanido kinase N-terminal domain

Domain ID domain_id	d1crka2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.128 — Glutamine synthetase/guanido kinase
Superfamily Superfamily superfamily	d.128.1 — Glutamine synthetase/guanido kinase
Family Family family	d.128.1.2 — Guanido kinase catalytic domain

Domain ID domain_id	d1crkb1
Class class	a — All alpha proteins
Fold Fold fold	a.83 — Guanido kinase N-terminal domain
Superfamily Superfamily superfamily	a.83.1 — Guanido kinase N-terminal domain
Family Family family	a.83.1.1 — Guanido kinase N-terminal domain

Domain ID domain_id	d1crkb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.128 — Glutamine synthetase/guanido kinase
Superfamily Superfamily superfamily	d.128.1 — Glutamine synthetase/guanido kinase
Family Family family	d.128.1.2 — Guanido kinase catalytic domain

Domain ID domain_id	d1crkc1
Class class	a — All alpha proteins
Fold Fold fold	a.83 — Guanido kinase N-terminal domain
Superfamily Superfamily superfamily	a.83.1 — Guanido kinase N-terminal domain
Family Family family	a.83.1.1 — Guanido kinase N-terminal domain

Domain ID domain_id	d1crkc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.128 — Glutamine synthetase/guanido kinase
Superfamily Superfamily superfamily	d.128.1 — Glutamine synthetase/guanido kinase
Family Family family	d.128.1.2 — Guanido kinase catalytic domain

Domain ID domain_id	d1crkd1
Class class	a — All alpha proteins
Fold Fold fold	a.83 — Guanido kinase N-terminal domain
Superfamily Superfamily superfamily	a.83.1 — Guanido kinase N-terminal domain
Family Family family	a.83.1.1 — Guanido kinase N-terminal domain

Domain ID domain_id	d1crkd2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.128 — Glutamine synthetase/guanido kinase
Superfamily Superfamily superfamily	d.128.1 — Glutamine synthetase/guanido kinase
Family Family family	d.128.1.2 — Guanido kinase catalytic domain

CATH v4.4 (8 domains)

Domain ID domain_id	1crkA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	135 — Transferase Creatine Kinase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — ATP:guanido phosphotransferase, N-terminal domain

Domain ID domain_id	1crkA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	1crkB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	135 — Transferase Creatine Kinase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — ATP:guanido phosphotransferase, N-terminal domain

Domain ID domain_id	1crkB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	1crkC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	135 — Transferase Creatine Kinase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — ATP:guanido phosphotransferase, N-terminal domain

Domain ID domain_id	1crkC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	1crkD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	135 — Transferase Creatine Kinase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — ATP:guanido phosphotransferase, N-terminal domain

Domain ID domain_id	1crkD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

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8. Citations (1)

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Unit-cell length a length_a	126.000 Å
Unit-cell length b length_b	126.000 Å
Unit-cell length c length_c	144.700 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 42
Space-group number int_tables_number	77
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2170
R_work r_work	0.2170
R_free r_free	0.2640

Description description	CREATINE KINASE
Molecular weight formula_weight	43259.4 kDa
EC 编号 ec_number	2.7.3.2
Source method src_method	nat
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	12184

MITOCHONDRIAL CREATINE KINASE

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

CREATINE KINASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	8

fit	/app/data/saxs_computation/cr/1crk/1crk.fit
pddf	/app/data/pr_computation/cr/1crk/1crk.pr.out
profile	/app/data/saxs_computation/cr/1crk/1crk.dat