SAXSdb — 1gzk

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

RAC-BETA SERINE/THREONINE PROTEIN KINASE

HOMO SAPIENS

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 146–460	Fragment：KINASE DOMAIN, RESIDUES (146 - 460)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；10MG/ML PROTEIN, 30% PEG4K, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, pH 7.50	Resolution 2.30 Å R-free 0.319

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.

Other PDB	Difference from Current Entry 1GZK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GZN Structure of PKB kinase domain Deposited 2002-05-24	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–480（335 aa） Fragment：KINASE DOMAIN AND HYDROPHOBIC MOTIF, RESIDUES 146-480	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；30% PEG 8K, 0.2 M LITHIUM SULPHATE 0.1 M TRIS, 10 MG/ML PROTEIN, pH 7.50	Resolution 2.50 Å R-free 0.319
1GZO Structure of protein kinase B unphosphorylated Deposited 2002-05-24	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–460（315 aa） Fragment：KINASE DOMAIN WITHOUT HYDROPHOBIC MOTIF, RESIDUES 146-460	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；30% PEG 8000, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, 10MG/ML PROTEIN, pH 7.50	Resolution 2.75 Å R-free 0.310
1MRV crystal structure of an inactive Akt2 kinase domain Deposited 2002-09-18	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 143–481（339 aa） Fragment：kinase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；Li2SO4, PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
1MRY crystal structure of an inactive akt2 kinase domain Deposited 2002-09-18	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 143–481（339 aa） Fragment：kinase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；Li2SO4, PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.272
1O6K Structure of activated form of PKB kinase domain S474D with GSK3 peptide and AMP-PNP Deposited 2002-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–481（336 aa） Fragment：KINASE DOMAIN, RESIDUES 146-481	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10 MG/ML PROTEIN 20 PEG 4K, 10% ISOPROPONAL, 5 MM DTT, pH 7.50	Resolution 1.70 Å R-free 0.234
1O6L Crystal structure of an activated Akt/protein kinase B (PKB-PIF chimera) ternary complex with AMP-PNP and GSK3 peptide Deposited 2002-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–467（322 aa） Fragment：KINASE DOMAIN, RESIDUES 146 - 467	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10 MG/ML PROTEIN, 20% (W/V) POLYETHYLENE, GLYCOL 4000, 10% (V/V) ISOPROPANOL, 0.1 M HEPES (PH 7.5), 5 MM DTT	Resolution 1.60 Å R-free 0.227
1P6S Solution Structure of the Pleckstrin Homology Domain of Human Protein Kinase B beta (Pkb/Akt) Deposited 2003-04-30	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–111（111 aa） Fragment：Pleckstrin Homology Domain (residues 1-111)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；286 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient NMR measurement conditions pH 7.4；286 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient NMR sample composition 0.4mM PKBbeta-PH U-15N,13C; 10mM Tris-HCl; 300mM NaCl; 0.1mM Benzamidine; 0.1mM EDTA; 4mM Inositol-1,4,5-trisphosphate; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.4mM PKBbeta-PH U-15N; 10mM Tris-HCl; 300mM NaCl; 0.1mM Benzamidine; 0.1mM EDTA; 4mM Inositol-1,4,5-trisphosphate; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2JDO STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE Deposited 2007-01-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467	Non-standard monomer：Yes (specific site not provided by mmCIF)	I5S ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.210
2JDR STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH THE INHIBITOR A-443654 Deposited 2007-01-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467	Non-standard monomer：Yes (specific site not provided by mmCIF)	L20 (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.252
2UW9 STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH 4-(4-chloro-phenyl)-4-(4-(1H-pyrazol-4-yl)-phenyl)-piperidine Deposited 2007-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467	Non-standard monomer：Yes (specific site not provided by mmCIF)	GVP 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.305
2X39 Structure of 4-Amino-N-(4-chlorobenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin- 4-yl)piperidine-4-carboxamide bound to PKB Deposited 2010-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–467（322 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467	Non-standard monomer：Yes (specific site not provided by mmCIF)	X39 4-AMINO-N-(4-CHLOROBENZYL)-1-(7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)PIPERIDINE-4-CARBOXAMIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.93 Å R-free 0.226
2XH5 Structure of 4-(4-tert-Butylbenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin-4- yl)piperidin-4-amine bound to PKB Deposited 2010-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–479（334 aa） Fragment：KINASE CATALYTIC DOMAIN, RESIDUES 146-467	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	X37 4-(4-tert-butylbenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.72 Å R-free 0.305
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 146–480（335 aa） Fragment：kinase domain Chain B 146–480（335 aa） Fragment：kinase domain	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K	Resolution 2.00 Å R-free 0.246
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–480（335 aa） Fragment：kinase domain	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K	Resolution 2.00 Å R-free 0.246
3D0E Crystal structure of human Akt2 in complex with GSK690693 Deposited 2008-05-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 146–480（335 aa） Fragment：kinase domain	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G93 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl}-2-methylbut-3 -yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 4K, 10% isopropanol, pH 8.0, vapor diffusion, temperature 298K	Resolution 2.00 Å R-free 0.246
3E87 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G95 N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.30 Å R-free 0.246
3E87 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G95 N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.30 Å R-free 0.246
3E88 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G96 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-6-{[(2R)-2-amino-3-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.50 Å R-free 0.273
3E88 Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 146–480（335 aa） Fragment：Akt2 kinase domain (146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G96 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-6-{[(2R)-2-amino-3-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.50 Å R-free 0.273
3E8D Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 146–480（335 aa） Fragment：Akt2 kinase domain (UNP residues 146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G98 4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.70 Å R-free 0.268
3E8D Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Deposited 2008-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 146–480（335 aa） Fragment：Akt2 kinase domain (UNP residues 146-480)	Mutation：S474D Non-standard monomer：Yes (specific site not provided by mmCIF)	G98 4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；14% PEG 2KMME, 100 mM Tris pH 8.0 and 10% ethanol diffused in. Seeded., vapor diffusion, temperature 298K	Resolution 2.70 Å R-free 0.268
8Q61 Co-crystal structure of human AKT2 with compound 3 Deposited 2023-08-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–481（481 aa）	Mutation：N2D	K06 6-[4-(1-azanyl-3-methyl-3-oxidanyl-cyclobutyl)phenyl]-7-phenyl-1-propyl-pyrido[2,3-b][1,4]oxazin-2-one × 1 GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 3 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M MES, 1.5 M NaH2PO4	Resolution 2.32 Å R-free 0.263
9C1W Structure of AKT2 with compound 3 Deposited 2024-05-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–447（446 aa）	Mutation：P115A, G116A	XOO 4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)amino]ethyl}-2-hydroxybenzaldehyde × 1 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M HEPES pH 7.5, 20 % w/v PEG 8000	Resolution 2.00 Å R-free 0.242

18 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AKT2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–315； UniProt 146–460

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1gzk
Deposition date deposition_date	2002-05-23
Structure title title	Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
Keywords keywords	KINASE, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING; KINASE
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	20.34 Å
Radius of gyration Rg (electron density) rg_electron	19.02 Å
Forward intensity I(0) i0	16240600.00
Molecular weight molecular_weight	31114.0 kDa
Excluded volume excluded_volume	39255 Å³
Envelope volume envelope_volume	46370 Å³
Hydration-shell volume shell_volume	20315 Å³
Envelope diameter envelope_diameter	64.4 Å
Shell Rg shell_rg	25.49 Å
Envelope Rg envelope_rg	19.18 Å
Shape Rg shape_rg	19.00 Å
Total Rg total_rg	20.06 Å
Total atoms total_atoms	2197
Residues n_residues	271
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	65.0 Å
Rg (real space) rg_real	20.24 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	1.6240e+07
I(0) uncertainty (real space) i0_real_error	2.1160e+05
Rg (reciprocal space) rg_reciprocal	20.26 Å
I(0) (reciprocal space) i0_reciprocal	16240000.0000
Solution quality estimate total_estimate	0.8961
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.0 Å
Skewness Skewness skewness	0.179
Kurtosis Kurtosis kurtosis	-0.440
Angular range angular_range	— – 0.3900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4168000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.892; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.976

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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) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1gzka_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (2 domains)

Domain ID domain_id	1gzkA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

Domain ID domain_id	1gzkA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

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8. Citations (1)

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Unit-cell length a length_a	148.405 Å
Unit-cell length b length_b	148.405 Å
Unit-cell length c length_c	38.547 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	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	34.980 Å
R factor r_factor	0.2480
R_work r_work	0.2480
R_free r_free	0.3190

Description description	RAC-BETA SERINE/THREONINE PROTEIN KINASE
Molecular weight formula_weight	36490.9 kDa
EC 编号 ec_number	2.7.1.-
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2481

Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation

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

RAC-BETA SERINE/THREONINE PROTEIN 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

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	SPODOPTERA FRUGIPERDA

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	284

fit	/app/data/saxs_computation/gz/1gzk/1gzk.fit
pddf	/app/data/pr_computation/gz/1gzk/1gzk.pr.out
profile	/app/data/saxs_computation/gz/1gzk/1gzk.dat