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1XCQ

Complex HCV core-Fab 19D9D6-Protein L mutant (D55A,L57H,Y64W) in space group P21

Summary for 1XCQ
Entry DOI10.2210/pdb1xcq/pdb
Related1XCT
DescriptorCapsid protein C, Monoclonal antibody 19D9D6 Light chain, Monoclonal antibody 19D9D6 Heavy chain, ... (5 entities in total)
Functional Keywordscrystal packing, fab, protein l, peptide complex, immune system
Biological sourceFinegoldia magna
More
Cellular locationCore protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P26661
Total number of polymer chains15
Total formula weight241930.98
Authors
Menez, R.,Housden, N.G.,Harrison, S.,Jolivet-Reynaud, C.,Gore, M.G.,Stura, E.A. (deposition date: 2004-09-03, release date: 2005-05-31, Last modification date: 2011-07-13)
Primary citationMenez, R.,Housden, N.G.,Harrison, S.,Jolivet-Reynaud, C.,Gore, M.G.,Stura, E.A.
Different crystal packing in Fab-protein L semi-disordered peptide complex.
Acta Crystallogr.,Sect.D, 61:744-749, 2005
Cited by
PubMed: 15930632
DOI: 10.1107/S0907444905006724
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

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