6M3B

hAPC-c25k23 Fab complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.220 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Targeted inhibition of activated protein C by a non-active-site inhibitory antibody to treat hemophilia.

Zhao, X.Y.Wilmen, A.Wang, D.Wang, X.Bauzon, M.Kim, J.Y.Linden, L.Li, L.Egner, U.Marquardt, T.Moosmayer, D.Tebbe, J.Gluck, J.M.Ellinger, P.McLean, K.Yuan, S.Yegneswaran, S.Jiang, X.Evans, V.Gu, J.M.Schneider, D.Zhu, Y.Xu, Y.Mallari, C.Hesslein, A.Wang, Y.Schmidt, N.Gutberlet, K.Ruehl-Fehlert, C.Freyberger, A.Hermiston, T.Patel, C.Sim, D.Mosnier, L.O.Laux, V.

(2020) Nat Commun 11: 2992-2992

  • DOI: https://doi.org/10.1038/s41467-020-16720-9
  • Primary Citation of Related Structures:  
    6M3B, 6M3C

  • PubMed Abstract: 

    Activated protein C (APC) is a plasma serine protease with antithrombotic and cytoprotective functions. Based on the hypothesis that specific inhibition of APC's anticoagulant but not its cytoprotective activity can be beneficial for hemophilia therapy, 2 types of inhibitory monoclonal antibodies (mAbs) are tested: A type I active-site binding mAb and a type II mAb binding to an exosite on APC (required for anticoagulant activity) as shown by X-ray crystallography. Both mAbs increase thrombin generation and promote plasma clotting. Type I blocks all APC activities, whereas type II preserves APC's cytoprotective function. In normal monkeys, type I causes many adverse effects including animal death. In contrast, type II is well-tolerated in normal monkeys and shows both acute and prophylactic dose-dependent efficacy in hemophilic monkeys. Our data show that the type II mAb can specifically inhibit APC's anticoagulant function without compromising its cytoprotective function and offers superior therapeutic opportunities for hemophilia.


  • Organizational Affiliation

    US Innovation Center, Bayer, 455 Mission Bay Blvd. South, San Francisco, CA, 94158, USA. xiao-yan.zhao@bayer.com.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Vitamin K-dependent protein C heavy chain250Homo sapiensMutation(s): 0 
Gene Names: PROC
EC: 3.4.21.69
UniProt & NIH Common Fund Data Resources
Find proteins for P04070 (Homo sapiens)
Explore P04070 
Go to UniProtKB:  P04070
PHAROS:  P04070
GTEx:  ENSG00000115718 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04070
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Vitamin K-dependent protein C light chainB [auth D]155Homo sapiensMutation(s): 0 
Gene Names: PROC
EC: 3.4.21.69
UniProt & NIH Common Fund Data Resources
Find proteins for P04070 (Homo sapiens)
Explore P04070 
Go to UniProtKB:  P04070
PHAROS:  P04070
GTEx:  ENSG00000115718 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04070
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
c25k23 Fab L chainC [auth B]214Homo sapiensMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
c25k23 Fab H chainD [auth C]223Homo sapiensMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NAG
Query on NAG

Download Ideal Coordinates CCD File 
E [auth A],
F [auth D]
2-acetamido-2-deoxy-beta-D-glucopyranose
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.220 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.277α = 90
b = 94.889β = 105.49
c = 114.32γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-07-08
    Type: Initial release
  • Version 1.1: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations, Structure summary
  • Version 1.2: 2023-11-29
    Changes: Data collection, Database references, Refinement description, Structure summary