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- PDB-2mcp: REFINED CRYSTAL STRUCTURE OF THE MC/PC603 FAB-PHOSPHOCHOLINE COMP... -

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Basic information

Entry
Database: PDB / ID: 2mcp
TitleREFINED CRYSTAL STRUCTURE OF THE MC/PC603 FAB-PHOSPHOCHOLINE COMPLEX AT 3.1 ANGSTROMS RESOLUTION
Components
  • IGA-KAPPA MCPC603 FAB (HEAVY CHAIN)
  • IGA-KAPPA MCPC603 FAB (LIGHT CHAIN)
KeywordsIMMUNE SYSTEM / IMMUNOGLOBULIN
Function / homology
Function and homology information


immunoglobulin complex / immunoglobulin mediated immune response / antigen binding
Similarity search - Function
Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold ...Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
PHOSPHOCHOLINE / : / Ig heavy chain V region M603
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / Resolution: 3.1 Å
AuthorsPadlan, E.A. / Cohen, G.H. / Davies, D.R.
Citation
Journal: To be Published
Title: Refined Crystal Structure of the Mc/Pc603 Fab-Phosphocholine Complex at 3.1 Angstroms Resolution
Authors: Padlan, E.A. / Cohen, G.H. / Davies, D.R.
#1: Journal: Ann.Immunol.(Paris),Sect.C / Year: 1985
Title: On the Specificity of Antibody(Slash)Antigen Interactions. Phosphocholine Binding to Mc/Pc603 and the Correlation of Three-Dimensional Structure and Sequence Data
Authors: Padlan, E.A. / Cohen, G.H. / Davies, D.R.
#2: Journal: The Immune System. Genes,Receptors,Signals. Proceedings of the 1974 I.C.N.-U.C.L.A. Symposium on Molecular Biology
Year: 1974
Title: The Three-Dimensional Structure of the Antigen Binding Site of Mc/Pc 603 Protein
Authors: Padlan, E.A. / Segal, D.M. / Cohen, G.H. / Davies, D.R. / Rudikoff, S. / Potter, M.
#3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1974
Title: The Three-Dimensional Structure of a Phosphorylcholine-Binding Mouse Immunoglobulin Fab and the Nature of the Antigen Binding Site
Authors: Segal, D.M. / Padlan, E.A. / Cohen, G.H. / Rudikoff, S. / Potter, M. / Davies, D.R.
#4: Journal: Nature New Biol. / Year: 1973
Title: Structure at 4.5 Angstroms Resolution of a Phosphorylcholine-Binding Fab Structure at 4.5 Angstroms Resolution of a Phosphorylcholine-Binding Fab
Authors: Padlan, E.A. / Segal, D.M. / Spande, T.F. / Rudikoff, D.R.Davies S. / Potter, M.
History
DepositionOct 15, 1984Processing site: BNL
Revision 1.0Jan 2, 1985Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Feb 8, 2017Group: Database references
Revision 2.0Jul 26, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other
Category: atom_site / atom_sites ...atom_site / atom_sites / database_2 / database_PDB_matrix / pdbx_database_remark / pdbx_database_status / pdbx_validate_rmsd_angle / pdbx_validate_symm_contact / pdbx_validate_torsion / struct_ref_seq_dif / struct_site
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[1][2] / _atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[2][2] / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _database_PDB_matrix.origx[1][1] / _database_PDB_matrix.origx[1][2] / _database_PDB_matrix.origx[2][1] / _database_PDB_matrix.origx[2][2] / _database_PDB_matrix.origx[3][3] / _pdbx_database_status.process_site / _pdbx_validate_rmsd_angle.angle_deviation / _pdbx_validate_rmsd_angle.angle_value / _pdbx_validate_symm_contact.dist / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Details: Coordinates and associated ncs operations (if present) transformed into standard crystal frame
Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
L: IGA-KAPPA MCPC603 FAB (LIGHT CHAIN)
H: IGA-KAPPA MCPC603 FAB (HEAVY CHAIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,6173
Polymers48,4332
Non-polymers1841
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4040 Å2
ΔGint-19 kcal/mol
Surface area19540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)162.531, 162.531, 60.719
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number173
Space group name H-MP63
Atom site foot note1: RESIDUES PRO L 8, PRO L 101, PRO L 147, PRO H 143 AND PRO H 155 ARE CIS PROLINES.

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Components

#1: Antibody IGA-KAPPA MCPC603 FAB (LIGHT CHAIN)


Mass: 24113.584 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / References: GenBank: 208622
#2: Antibody IGA-KAPPA MCPC603 FAB (HEAVY CHAIN)


Mass: 24319.266 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / References: UniProt: P01789
#3: Chemical ChemComp-PC / PHOSPHOCHOLINE / Phosphocholine


Mass: 184.151 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H15NO4P

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 4.78 Å3/Da / Density % sol: 74.25 %

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

RefinementRfactor Rwork: 0.185 / Highest resolution: 3.1 Å
Refinement stepCycle: LAST / Highest resolution: 3.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3401 0 11 0 3412

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