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PDB: 8 results

1CCF
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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
Descriptor: COAGULATION FACTOR X
Authors:Selander-Sunnerhagen, M, Ullner, M, Persson, M, Teleman, O, Stenflo, J, Drakenberg, T.
Deposit date:1993-05-19
Release date:1994-05-31
Last modified:2023-11-15
Method:SOLUTION NMR
Cite: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.
J.Biol.Chem., 267, 1992
1APO
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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
Descriptor: EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X, HYDROXIDE ION
Authors:Ullner, M, Selander, M, Persson, E, Stenflo, J, Drakenberg, T, Teleman, O.
Deposit date:1992-04-21
Release date:1994-01-31
Last modified:2017-11-29
Method:SOLUTION NMR
Cite: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.
Biochemistry, 31, 1992
1BF9
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N-TERMINAL EGF-LIKE DOMAIN FROM HUMAN FACTOR VII, NMR, 23 STRUCTURES
Descriptor: FACTOR VII
Authors:Muranyi, A, Finn, B.E, Gippert, G.P, Forsen, S, Stenflo, J, Drakenberg, T.
Deposit date:1998-05-28
Release date:1999-02-16
Last modified:2017-11-29
Method:SOLUTION NMR
Cite:Solution structure of the N-terminal EGF-like domain from human factor VII.
Biochemistry, 37, 1998
1WHF
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COAGULATION FACTOR, NMR, 15 STRUCTURES
Descriptor: COAGULATION FACTOR X
Authors:Sunnerhagen, M, Olah, G.A, Stenflo, J, Forsen, S, Drakenberg, T, Trewhella, J.
Deposit date:1996-06-18
Release date:1997-05-15
Last modified:2017-11-29
Method:SOLUTION NMR
Cite: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.
Biochemistry, 35, 1996
1WHE
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COAGULATION FACTOR, NMR, 20 STRUCTURES
Descriptor: COAGULATION FACTOR X
Authors:Sunnerhagen, M, Olah, G.A, Stenflo, J, Forsen, S, Drakenberg, T, Trewhella, J.
Deposit date:1996-06-18
Release date:1997-05-15
Last modified:2017-11-29
Method:SOLUTION NMR
Cite: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.
Biochemistry, 35, 1996
1Z6C
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Solution structure of an EGF pair (EGF34) from vitamin K-dependent protein S
Descriptor: CALCIUM ION, Vitamin K-dependent protein S
Authors:Drakenberg, T, Ghasriani, H, Thulin, E, Thamlitz, A.M, Muranyi, A, Annila, A, Stenflo, J.
Deposit date:2005-03-22
Release date:2005-06-21
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:Solution Structure of the Ca(2+)-Binding EGF3-4 Pair from Vitamin K-Dependent Protein S: Identification of an Unusual Fold in EGF3.
Biochemistry, 44, 2005
1LQ8
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Crystal structure of cleaved protein C inhibitor
Descriptor: 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ...
Authors:Huntington, J.A, Kjellberg, M, Stenflo, J.
Deposit date:2002-05-09
Release date:2003-02-11
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Crystal Structure of Protein C Inhibitor Provides Insights into Hormone Binding and Heparin Activation
Structure, 11, 2003
1WCT
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A NOVEL CONOTOXIN FROM CONUS TEXTILE WITH UNUSUAL POST-TRANSLATIONAL MODIFICATIONS REDUCES PRESYNAPTIC CALCIUM INFLUX, NMR, 1 STRUCTURE, GLYCOSYLATED PROTEIN
Descriptor: OMEGAC-TXIX, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose
Authors:Rigby, A.C, Hambe, B, Czerwiec, E, Baleja, J.D, Furie, B.C, Furie, B, Stenflo, J.
Deposit date:1998-12-18
Release date:1999-06-08
Last modified:2020-07-29
Method:SOLUTION NMR
Cite:A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influx.
Proc.Natl.Acad.Sci.USA, 96, 1999

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