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- PDB-1whe: COAGULATION FACTOR, NMR, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1whe
TitleCOAGULATION FACTOR, NMR, 20 STRUCTURES
ComponentsCOAGULATION FACTOR X
KeywordsGLYCOPROTEIN / HYDROLASE / SERINE PROTEASE / PLASMA / BLOOD COAGULATION FACTOR
Function / homology
Function and homology information


coagulation factor Xa / blood coagulation / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space
Similarity search - Function
Coagulation Factor IX / Coagulation Factor IX / Peptidase S1A, coagulation factor VII/IX/X/C/Z / : / Coagulation factor-like, Gla domain superfamily / Laminin / Laminin / Coagulation Factor Xa inhibitory site / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site ...Coagulation Factor IX / Coagulation Factor IX / Peptidase S1A, coagulation factor VII/IX/X/C/Z / : / Coagulation factor-like, Gla domain superfamily / Laminin / Laminin / Coagulation Factor Xa inhibitory site / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like 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. / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Ribbon / Few Secondary Structures / Irregular / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Mainly Beta
Similarity search - Domain/homology
Coagulation factor X
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodSOLUTION NMR
AuthorsSunnerhagen, M. / Olah, G.A. / Stenflo, J. / Forsen, S. / Drakenberg, T. / Trewhella, J.
Citation
Journal: Biochemistry / Year: 1996
Title: The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
Authors: Sunnerhagen, M. / Olah, G.A. / Stenflo, J. / Forsen, S. / Drakenberg, T. / Trewhella, J.
#1: Journal: Nat.Struct.Biol. / Year: 1995
Title: Structure of the Ca(2+)-Free Gla Domain Sheds Light on Membrane Binding of Blood Coagulation Proteins
Authors: Sunnerhagen, M. / Forsen, S. / Hoffren, A.M. / Drakenberg, T. / Teleman, O. / Stenflo, J.
#2: Journal: J.Biol.Chem. / Year: 1992
Title: How an Epidermal Growth Factor (Egf)-Like Domain Binds Calcium. High Resolution NMR Structure of the Calcium Form of the NH2-Terminal Egf-Like Domain in Coagulation Factor X
Authors: Selander-Sunnerhagen, M. / Ullner, M. / Persson, E. / Teleman, O. / Stenflo, J. / Drakenberg, T.
#3: Journal: Biochemistry / Year: 1992
Title: Three-Dimensional Structure of the Apo Form of the N-Terminal Egf-Like Module of Blood Coagulation Factor X as Determined by NMR Spectroscopy and Simulated Folding
Authors: Ullner, M. / Selander, M. / Persson, E. / Stenflo, J. / Drakenberg, T. / Teleman, O.
History
DepositionJun 18, 1996Processing site: BNL
Revision 1.0May 15, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 20, 2012Group: Non-polymer description
Revision 1.4Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.5Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: COAGULATION FACTOR X


Theoretical massNumber of molelcules
Total (without water)10,2941
Polymers10,2941
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein COAGULATION FACTOR X


Mass: 10293.607 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: THE APO FORM OF THE FRAGMENT CONTAINING THE GLA AND N-TERMINAL EGF-LIKE MODULE
Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00743, coagulation factor Xa
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 20

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