5I4E

Crystal Structure of Human Nonmuscle Myosin 2C motor domain

Replaces:  2YCU

> Summary

Summary for 5I4E

DescriptorMyosin-14,Alpha-actinin A, ADP ORTHOVANADATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsmotor protein
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm  P05095
Total number of polymer chains1
Total molecular weight112157.25
Authors
Chinthalapudi, K.,Heissler, S.M.,Preller, M.,Sellers, J.R.,Manstein, D.J. (deposition date: 2016-02-11, release date: 2017-09-13)
Primary citation
Chinthalapudi, K.,Heissler, S.M.,Preller, M.,Sellers, J.R.,Manstein, D.J.
Allosteric Regulation of Myosin Function: Insights from the Crystal Structure of the Human Nonmuscle Myosin-2C Motor Domain
To be published,
Experimental method
X-RAY DIFFRACTION (2.25 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.260140.2%0.8%14.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 5i4e
no rotation
Molmil generated image of 5i4e
rotated about x axis by 90°
Molmil generated image of 5i4e
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
AMyosin-14,Alpha-actinin Apolymer980111588.81
UniProt (Q7Z406)
UniProt (P05095)
Homo sapiens (Human)Myosin heavy chain 14,Myosin heavy chain,non-muscle IIc,Non-muscle myosin heavy chain IIc,NMHC II-C,Actin-binding protein A,F-actin cross-linking protein
ADP ORTHOVANADATEnon-polymer544.21
MAGNESIUM IONnon-polymer24.31
waterwater18.0665

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight111588.8
Non-Polymers*Number of molecules2
Total molecular weight568.5
All*Total molecular weight112157.3
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.25 Å)

Cell axes81.120125.610153.960
Cell angles90.0090.0090.00
SpacegroupP 2 21 21
Resolution limits34.77 - 2.25
the highest resolution shell value2.310 - 2.250
R-factor0.221
R-work0.22000
the highest resolution shell value0.292
R-free0.24100
the highest resolution shell value0.291
RMSD bond length0.010
RMSD bond angle1.160

Data Collection Statistics

Resolution limits97.33 - 2.25
the highest resolution shell value -
Number of reflections75357
Rmerge_l_obs0.120
the highest resolution shell value0.230
Completeness99.8
Redundancy14.82
the highest resolution shell value14.97

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP281.15

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC123binding site for residue AOV A 1500
ChainResidue
AASN146
ATYR148
ALYS149
ATYR154
ASER200
AGLY201
AALA202
AGLY203
ALYS204
ATHR205
AGLU206
AASN256
ASER259
ASER260
AGLY481
AMG1501
AHOH1609
AHOH1612
AHOH1634
AHOH1639
AHOH1680
AHOH1782
AHOH1797

AC25binding site for residue MG A 1501
ChainResidue
ATHR205
ASER260
AAOV1500
AHOH1609
AHOH1639

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
AOV_5i4e_A_150029ADP ORTHOVANADATE binding site
ChainResidueligand
AILE134-TYR135AOV: ADP ORTHOVANADATE
AASN146-GLN150AOV: ADP ORTHOVANADATE
ATYR154AOV: ADP ORTHOVANADATE
AGLY198-ASN207AOV: ADP ORTHOVANADATE
AASN256AOV: ADP ORTHOVANADATE
AASN258-ARG261AOV: ADP ORTHOVANADATE
AASP478-GLU483AOV: ADP ORTHOVANADATE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI1122
ChainResidueDetails
ANA*

SWS_FT_FI2121
ChainResidueDetails
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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