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- PDB-7p6p: ROCK2 IN COMPLEX WITH COMPOUND 17 -

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Basic information

Entry
Database: PDB / ID: 7p6p
TitleROCK2 IN COMPLEX WITH COMPOUND 17
ComponentsRho-associated protein kinase 2
KeywordsTRANSFERASE / Rho-associated protein kinase 2 / inhibitor complex
Function / homology
Function and homology information


positive regulation of connective tissue growth factor production / cellular response to acetylcholine / positive regulation of fibroblast growth factor production / positive regulation of centrosome duplication / regulation of angiotensin-activated signaling pathway / negative regulation of protein localization to lysosome / regulation of keratinocyte differentiation / Rho-dependent protein serine/threonine kinase activity / positive regulation of connective tissue replacement / response to transforming growth factor beta ...positive regulation of connective tissue growth factor production / cellular response to acetylcholine / positive regulation of fibroblast growth factor production / positive regulation of centrosome duplication / regulation of angiotensin-activated signaling pathway / negative regulation of protein localization to lysosome / regulation of keratinocyte differentiation / Rho-dependent protein serine/threonine kinase activity / positive regulation of connective tissue replacement / response to transforming growth factor beta / positive regulation of amyloid precursor protein catabolic process / regulation of cell junction assembly / regulation of nervous system process / positive regulation of protein localization to early endosome / host-mediated perturbation of viral process / cellular response to testosterone stimulus / regulation of cellular response to hypoxia / embryonic morphogenesis / negative regulation of nitric oxide biosynthetic process / regulation of cell motility / negative regulation of biomineral tissue development / regulation of establishment of endothelial barrier / response to angiotensin / regulation of stress fiber assembly / RHO GTPases Activate ROCKs / actomyosin structure organization / Sema4D induced cell migration and growth-cone collapse / aortic valve morphogenesis / cortical actin cytoskeleton organization / RHOBTB1 GTPase cycle / regulation of establishment of cell polarity / negative regulation of bicellular tight junction assembly / tau-protein kinase activity / regulation of focal adhesion assembly / RHOB GTPase cycle / positive regulation of amyloid-beta formation / EPHA-mediated growth cone collapse / positive regulation of cardiac muscle hypertrophy / RHOC GTPase cycle / mRNA destabilization / centrosome duplication / mitotic cytokinesis / RHOH GTPase cycle / smooth muscle contraction / epithelial to mesenchymal transition / RHOA GTPase cycle / endopeptidase activator activity / regulation of cell adhesion / Rho protein signal transduction / positive regulation of stress fiber assembly / EPHB-mediated forward signaling / positive regulation of endothelial cell migration / blood vessel diameter maintenance / negative regulation of angiogenesis / response to ischemia / protein localization to plasma membrane / regulation of actin cytoskeleton organization / regulation of circadian rhythm / small GTPase binding / VEGFA-VEGFR2 Pathway / tau protein binding / cytoplasmic ribonucleoprotein granule / positive regulation of protein phosphorylation / rhythmic process / G alpha (12/13) signalling events / actin cytoskeleton organization / protease binding / Potential therapeutics for SARS / cytoskeleton / protein phosphorylation / non-specific serine/threonine protein kinase / positive regulation of MAPK cascade / positive regulation of cell migration / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / positive regulation of gene expression / structural molecule activity / RNA binding / zinc ion binding / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
: / Rho-associated protein kinase 2, HR1 domain / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / MRCK kinase PH domain / : / HR1 rho-binding domain / REM-1 domain profile. ...: / Rho-associated protein kinase 2, HR1 domain / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / MRCK kinase PH domain / : / HR1 rho-binding domain / REM-1 domain profile. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
: / Rho-associated protein kinase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.82 Å
AuthorsMaillard, M.C.
CitationJournal: J.Med.Chem. / Year: 2022
Title: Identification of a Potent, Selective, and Brain-Penetrant Rho Kinase Inhibitor and its Activity in a Mouse Model of Huntington's Disease.
Authors: Ladduwahetty, T. / Lee, M.R. / Maillard, M.C. / Cachope, R. / Todd, D. / Barnes, M. / Beaumont, V. / Chauhan, A. / Gallati, C. / Haughan, A.F. / Kempf, G. / Luckhurst, C.A. / Matthews, K. / ...Authors: Ladduwahetty, T. / Lee, M.R. / Maillard, M.C. / Cachope, R. / Todd, D. / Barnes, M. / Beaumont, V. / Chauhan, A. / Gallati, C. / Haughan, A.F. / Kempf, G. / Luckhurst, C.A. / Matthews, K. / McAllister, G. / Mitchell, P. / Patel, H. / Rose, M. / Saville-Stones, E. / Steinbacher, S. / Stott, A.J. / Thatcher, E. / Tierney, J. / Urbonas, L. / Munoz-Sanjuan, I. / Dominguez, C.
History
DepositionJul 16, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 22, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Rho-associated protein kinase 2
B: Rho-associated protein kinase 2
C: Rho-associated protein kinase 2
D: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)184,58311
Polymers182,8044
Non-polymers1,7807
Water70339
1
A: Rho-associated protein kinase 2
B: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,3096
Polymers91,4022
Non-polymers9084
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4290 Å2
ΔGint-31 kcal/mol
Surface area36080 Å2
MethodPISA
2
C: Rho-associated protein kinase 2
D: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,2745
Polymers91,4022
Non-polymers8723
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4180 Å2
ΔGint-18 kcal/mol
Surface area35900 Å2
MethodPISA
Unit cell
Length a, b, c (Å)151.029, 133.077, 92.826
Angle α, β, γ (deg.)90.000, 109.240, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: ARG / End label comp-ID: ARG / Refine code: _ / Auth seq-ID: 24 - 417 / Label seq-ID: 6 - 399

Dom-IDEns-IDAuth asym-IDLabel asym-ID
11AA
21BB
12AA
22CC
13AA
23DD
14BB
24CC
15BB
25DD
16CC
26DD

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein
Rho-associated protein kinase 2 / Rho kinase 2 / Rho-associated / coiled-coil-containing protein kinase 2 / coiled-coil-containing ...Rho kinase 2 / Rho-associated / coiled-coil-containing protein kinase 2 / coiled-coil-containing protein kinase II / ROCK-II / p164 ROCK-2


Mass: 45700.914 Da / Num. of mol.: 4 / Fragment: KINASE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ROCK2, KIAA0619 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: O75116, non-specific serine/threonine protein kinase
#2: Chemical
ChemComp-5YV / ~{N}-[(1~{R})-1-(3-methoxyphenyl)ethyl]-4-pyridin-4-yl-cyclohexane-1-carboxamide


Mass: 338.443 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H26N2O2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 39 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 50.51 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.25 / Details: PEG6000, LiCl, MES/NaOH

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00004291534 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 7, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00004291534 Å / Relative weight: 1
ReflectionResolution: 2.82→97.29 Å / Num. obs: 40561 / % possible obs: 96.5 % / Redundancy: 4.1 % / Biso Wilson estimate: 73.667 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.78 / Rrim(I) all: 0.089 / Χ2: 1.073 / Net I/σ(I): 12.25
Reflection shellResolution: 2.82→3.07 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.448 / Mean I/σ(I) obs: 3.07 / Num. unique obs: 165 / CC1/2: 0.995 / Rrim(I) all: 0.051 / % possible all: 86.4

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Processing

Software
NameVersionClassification
XSCALEdata scaling
REFMAC5.8.0155refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: NONE

Resolution: 2.82→97.29 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.911 / SU B: 42 / SU ML: 0.38 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.408 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2584 677 1.7 %RANDOM
Rwork0.2217 ---
obs0.2224 39840 96.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 215.37 Å2 / Biso mean: 79.591 Å2 / Biso min: 32.04 Å2
Baniso -1Baniso -2Baniso -3
1--6.23 Å2-0 Å2-2.4 Å2
2--7.81 Å2-0 Å2
3---0.08 Å2
Refinement stepCycle: final / Resolution: 2.82→97.29 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12406 0 125 39 12570
Biso mean--68.02 57.34 -
Num. residues----1524
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01912351
X-RAY DIFFRACTIONr_bond_other_d0.0030.0211410
X-RAY DIFFRACTIONr_angle_refined_deg1.5571.95816771
X-RAY DIFFRACTIONr_angle_other_deg1.25326058
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.66251509
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.33623.924576
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.037151906
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.8191567
X-RAY DIFFRACTIONr_chiral_restr0.0920.21820
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.02114057
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022956
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A229700.05
12B229700.05
21A234980.05
22C234980.05
31A236700.06
32D236700.06
41B229780.04
42C229780.04
51B229000.04
52D229000.04
61C232200.05
62D232200.05
LS refinement shellResolution: 2.82→2.893 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.435 24 -
Rwork0.417 1998 -
obs--65.18 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.03111.05580.7790.410.65131.8285-0.13680.268-0.1501-0.05210.14760.0229-0.02380.2958-0.01080.2782-0.03160.12610.1006-0.01430.446750.0227.31719.927
23.22592.58610.06544.4855-0.22732.93260.00250.17540.1421-0.02160.1257-0.2501-0.35260.0634-0.12810.14840.05640.14870.04910.08140.218228.5854.32615.958
33.7687-0.8023-0.70682.6458-0.09332.19680.0471-0.52410.27020.5965-0.1655-0.2134-0.20360.06450.11850.2043-0.02540.02760.15790.05010.15699.85-3.47630.893
43.33111.89290.99662.82441.11791.6725-0.04490.34390.2063-0.22330.0889-0.1061-0.19830.0326-0.0440.16840.02410.16920.04440.050.196523.6640.10616.719
56.0133-1.99941.23672.1979-1.60611.1888-0.1363-0.3891-0.25830.20980.23730.1674-0.1614-0.156-0.10110.3294-0.09270.24080.0906-0.00030.41751.5385.70426.48
63.8925-1.38950.12153.962-0.19282.5023-0.1295-0.08550.30140.30260.11270.0209-0.26540.17580.01680.1868-0.13680.08090.1834-0.05340.090873.3485.55528.947
73.63371.3550.20594.17480.10323.9651-0.20520.65950.6332-0.05140.0416-0.5018-0.62910.58830.16360.2699-0.20250.08390.4970.0820.396193.30310.64214.279
83.7179-1.16331.07021.5849-0.93940.6412-0.0854-0.61770.22070.21750.0636-0.1069-0.1755-0.02170.02170.3086-0.10760.16730.3858-0.15080.280178.6164.15926.777
91.91860.71091.95831.25130.49353.5322-0.2430.17310.1521-0.08740.180.0703-0.55580.12610.0630.2993-0.04830.08970.0508-0.01910.2695-19.08739.5438.209
104.66171.30261.66152.47030.73613.9953-0.01710.251-0.307-0.00330.2036-0.0303-0.24950.2965-0.18650.1466-0.02160.10470.1511-0.04110.1001-0.14439.76519.404
111.8094-0.41060.21324.3882-0.48983.2125-0.0348-0.2474-0.47670.66370.112-0.28610.03580.117-0.07730.39490.00770.0130.3257-0.03960.20946.8533.34642.888
123.66812.28683.21353.36412.28742.90090.00430.2162-0.3110.33150.2521-0.36170.02630.2856-0.25630.2734-0.06060.10180.20010.00380.20112.60740.85324.297
135.3515-0.61740.99110.19160.3472.0908-0.2285-0.47660.01420.00340.10080.044-0.28220.03740.12770.33210.06070.09330.09-0.02170.2479-24.28236.8312.34
144.2423-1.3469-0.94043.4972-0.66643.656-0.03970.2354-0.1904-0.02160.0594-0.18920.10550.1324-0.01970.0627-0.04560.01730.0835-0.01510.1345-43.65939.6592.345
151.9967-0.40631.56631.8716-0.56983.33120.16970.5673-0.3581-0.2263-0.1006-0.37220.23160.6316-0.06910.18290.04370.12570.2733-0.0590.2756-50.3149.361-20.119
163.7148-1.40680.87210.8675-0.44831.03340.00410.0153-0.3790.09480.06020.0189-0.12260.0067-0.06440.1901-0.00460.12170.0976-0.03310.2479-47.25944.077-0.919
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 91
2X-RAY DIFFRACTION2A92 - 170
3X-RAY DIFFRACTION3A171 - 355
4X-RAY DIFFRACTION4A356 - 450
5X-RAY DIFFRACTION5B1 - 91
6X-RAY DIFFRACTION6B92 - 170
7X-RAY DIFFRACTION7B171 - 355
8X-RAY DIFFRACTION8B356 - 450
9X-RAY DIFFRACTION9C1 - 91
10X-RAY DIFFRACTION10C92 - 170
11X-RAY DIFFRACTION11C171 - 355
12X-RAY DIFFRACTION12C356 - 450
13X-RAY DIFFRACTION13D1 - 91
14X-RAY DIFFRACTION14D92 - 170
15X-RAY DIFFRACTION15D171 - 355
16X-RAY DIFFRACTION16D356 - 450

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