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- PDB-2pf2: THE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF ... -

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Basic information

Entry
Database: PDB / ID: 2pf2
TitleTHE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF CA-PROTHROMBIN FRAGMENT 1
ComponentsPROTHROMBIN FRAGMENT 1
KeywordsHYDROLASE(SERINE PROTEASE)
Function / homology
Function and homology information


fibrinogen binding / thrombin / protein polymerization / positive regulation of blood coagulation / acute-phase response / platelet activation / collagen-containing extracellular matrix / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space
Similarity search - Function
Plasminogen Kringle 4 / Plasminogen Kringle 4 / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily ...Plasminogen Kringle 4 / Plasminogen Kringle 4 / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Kringle-like fold / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / Resolution: 2.2 Å
AuthorsSoriano-Garcia, M. / Padmanabhan, K. / De vos, A.M. / Tulinsky, A.
Citation
Journal: Biochemistry / Year: 1992
Title: The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1.
Authors: Soriano-Garcia, M. / Padmanabhan, K. / de Vos, A.M. / Tulinsky, A.
#1: Journal: J.Mol.Biol. / Year: 1991
Title: Structure of Bovine Prothrombin Fragment 1 Refined at 2.25 Angstroms Resolution
Authors: Seshadri, T.P. / Tulinsky, A. / Skrzypczak-Jankun, E. / Park, C.H.
#2: Journal: Biochemistry / Year: 1989
Title: Structure of Ca2+ Prothrombin Fragment 1 Including the Conformation of the Gla Domain
Authors: Soriano-Garcia, M. / Park, C.H. / Tulinsky, A. / Ravichandran, K.G. / Skrzypczak-Jankun, E.
History
DepositionDec 8, 1991Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTHROMBIN FRAGMENT 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,3058
Polymers18,0251
Non-polymers2817
Water2,594144
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)39.390, 53.880, 129.640
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Atom site foot note1: RESIDUES PRO 54 AND PRO 95 ARE CIS PROLINES.

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Components

#1: Protein PROTHROMBIN FRAGMENT 1


Mass: 18024.672 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00735
#2: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Ca
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 144 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.81 Å3/Da / Density % sol: 67.75 %
Crystal grow
*PLUS
pH: 6.5 / Method: vapor diffusion, hanging drop
Details: taken from Soriano-Garacia, M. et al (1989), Biochemistry, 28, 6805-6810.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
10.1 Mcacodylate1drop
28 %(w/v)PEG60001drop
3100 mM1dropCa2+
416 %(w/v)PEG60001reservoir
50.1 Mcacodylate1reservoir
6200 mM1reservoirCa2+

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2.2 Å / Num. all: 12662 / Num. obs: 8141 / % possible obs: 64 %

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Processing

Software
NameClassification
X-PLORmodel building
PROFFTrefinement
PROLSQrefinement
X-PLORrefinement
X-PLORphasing
RefinementResolution: 2.2→7 Å / Rfactor obs: 0.171 / σ(F): 1
Refinement stepCycle: LAST / Resolution: 2.2→7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1166 0 7 144 1317
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0170.02
X-RAY DIFFRACTIONp_angle_d0.0550.04
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.060.05
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it1.11.5
X-RAY DIFFRACTIONp_mcangle_it1.82
X-RAY DIFFRACTIONp_scbond_it1.72
X-RAY DIFFRACTIONp_scangle_it2.52.5
X-RAY DIFFRACTIONp_plane_restr0.0220.03
X-RAY DIFFRACTIONp_chiral_restr0.1870.15
X-RAY DIFFRACTIONp_singtor_nbd0.240.6
X-RAY DIFFRACTIONp_multtor_nbd0.330.6
X-RAY DIFFRACTIONp_xhyhbond_nbd0.340.6
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor3.13
X-RAY DIFFRACTIONp_staggered_tor2615
X-RAY DIFFRACTIONp_orthonormal_tor1820
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: PROLSQ / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.2 Å / Lowest resolution: 7 Å / Num. reflection obs: 1024 / σ(F): 1 / Rfactor obs: 0.171
Solvent computation
*PLUS
Displacement parameters
*PLUS

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