6RLX

X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS

> Summary

Summary for 6RLX

DescriptorRELAXIN
Functional Keywordshormone(muscle relaxant)
Biological sourceHomo sapiens (human)
Cellular locationSecreted P04090 P04090
Total number of polymer chains4
Total molecular weight11723.99
Authors
Eigenbrot, C.,Randal, M.,Kossiakoff, A.A. (deposition date: 1991-06-21, release date: 1993-10-31, modification date: 2011-11-16)
Primary citation
Eigenbrot, C.,Randal, M.,Quan, C.,Burnier, J.,O'Connell, L.,Rinderknecht, E.,Kossiakoff, A.A.
X-ray structure of human relaxin at 1.5 A. Comparison to insulin and implications for receptor binding determinants.
J.Mol.Biol., 221:15-21, 1991
PubMed: 1656049
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.5 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers506.2%6.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 6rlx
no rotation
Molmil generated image of 6rlx
rotated about x axis by 90°
Molmil generated image of 6rlx
rotated about y axis by 90°

> Structural details

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains4
Total molecular weight11724.0
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight11724.0
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (1.5 Å)

Cell axes53.97056.88061.680
Cell angles90.0090.0090.00
SpacegroupC 2 2 21
Resolution limits - 1.50
the highest resolution shell value -
R-factor0.187
R-work0.18700
RMSD bond length0.021
RMSD bond angle3.000

Data Collection Statistics

Resolution limits - 1.50*
the highest resolution shell value -
Number of reflections13471*
Number of measurements50106*
Rmerge_l_obs0.063*

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1Vapor diffusion*5.0*unknown*

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
11droprelaxin5 (mg/ml)
21reservoir150 (mM)
31reservoircitrate10 (mM)
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0007565biological_processfemale pregnancy
A0045766biological_processpositive regulation of angiogenesis
A0030819biological_processpositive regulation of cAMP biosynthetic process
A0010628biological_processpositive regulation of gene expression
A0050790biological_processregulation of catalytic activity
C0005576cellular_componentextracellular region
C0007565biological_processfemale pregnancy
C0045766biological_processpositive regulation of angiogenesis
C0030819biological_processpositive regulation of cAMP biosynthetic process
C0010628biological_processpositive regulation of gene expression
C0050790biological_processregulation of catalytic activity
B0005576cellular_componentextracellular region
B0007565biological_processfemale pregnancy
B0045766biological_processpositive regulation of angiogenesis
B0030819biological_processpositive regulation of cAMP biosynthetic process
B0010628biological_processpositive regulation of gene expression
B0050790biological_processregulation of catalytic activity
D0005576cellular_componentextracellular region
D0007565biological_processfemale pregnancy
D0045766biological_processpositive regulation of angiogenesis
D0030819biological_processpositive regulation of cAMP biosynthetic process
D0010628biological_processpositive regulation of gene expression
D0050790biological_processregulation of catalytic activity
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Functional Information from PDB Data

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

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Functional Information from PROSITE/UniProt

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Functional Information from SwissProt/UniProt

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Catalytic Information from CSA

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Catalytic Information from CATRES

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> Sequence Neighbor

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