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1lj7

Crystal structure of calcium-depleted human C-reactive protein from perfectly twinned data

Method: X-RAY DIFFRACTION Dmax: 119.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

C-reactive protein

OrganismNot specified

UniProt P02741

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain A； UniProt 19–224 Chain B； UniProt 19–224 Chain C； UniProt 19–224 Chain D； UniProt 19–224 Chain E； UniProt 19–224 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP Resolution 3.15 Å R-free 0.199
2 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain F； UniProt 19–224 Chain G； UniProt 19–224 Chain H； UniProt 19–224 Chain I； UniProt 19–224 Chain J； UniProt 19–224 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP Resolution 3.15 Å R-free 0.199

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1LJ7 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B09 HUMAN C-REACTIVE PROTEIN COMPLEXED WITH PHOSPHOCHOLINE Deposited 1998-11-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 PC PHOSPHOCHOLINE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6；pH 7.6
Resolution 2.50 Å R-free 0.242
1GNH HUMAN C-REACTIVE PROTEIN Deposited 1996-03-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.00 Å R-free 0.273
1GNH HUMAN C-REACTIVE PROTEIN Deposited 1996-03-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.00 Å R-free 0.273
3L2Y The structure of C-reactive protein bound to phosphoethanolamine Deposited 2009-12-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；285.15 K；0.06M TRIS-HCL pH7.5, 10% MPD, 0.01M CaCl2, 0.14M NaCl, 0.1% NaN3, 0.1% LM AGAROSE, VAPOR DIFFUSION, HANGING DROP, temperature 285.15K
Resolution 2.70 Å R-free 0.246
3L2Y The structure of C-reactive protein bound to phosphoethanolamine Deposited 2009-12-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；285.15 K；0.06M TRIS-HCL pH7.5, 10% MPD, 0.01M CaCl2, 0.14M NaCl, 0.1% NaN3, 0.1% LM AGAROSE, VAPOR DIFFUSION, HANGING DROP, temperature 285.15K
Resolution 2.70 Å R-free 0.246
3L2Y The structure of C-reactive protein bound to phosphoethanolamine Deposited 2009-12-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain K 19–224（206 aa）
Chain L 19–224（206 aa）
Chain M 19–224（206 aa）
Chain N 19–224（206 aa）
Chain O 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；285.15 K；0.06M TRIS-HCL pH7.5, 10% MPD, 0.01M CaCl2, 0.14M NaCl, 0.1% NaN3, 0.1% LM AGAROSE, VAPOR DIFFUSION, HANGING DROP, temperature 285.15K
Resolution 2.70 Å R-free 0.246
3L2Y The structure of C-reactive protein bound to phosphoethanolamine Deposited 2009-12-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain P 19–224（206 aa）
Chain Q 19–224（206 aa）
Chain R 19–224（206 aa）
Chain S 19–224（206 aa）
Chain T 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；285.15 K；0.06M TRIS-HCL pH7.5, 10% MPD, 0.01M CaCl2, 0.14M NaCl, 0.1% NaN3, 0.1% LM AGAROSE, VAPOR DIFFUSION, HANGING DROP, temperature 285.15K
Resolution 2.70 Å R-free 0.246
3PVN Triclinic form of Human C-Reactive Protein in complex with Zinc Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa） Fragment：UNP residues 19-224
Chain B 19–224（206 aa） Fragment：UNP residues 19-224
Chain C 19–224（206 aa） Fragment：UNP residues 19-224
Chain D 19–224（206 aa） Fragment：UNP residues 19-224
Chain E 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-Hcl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 1.98 Å R-free 0.236
3PVN Triclinic form of Human C-Reactive Protein in complex with Zinc Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa） Fragment：UNP residues 19-224
Chain G 19–224（206 aa） Fragment：UNP residues 19-224
Chain H 19–224（206 aa） Fragment：UNP residues 19-224
Chain I 19–224（206 aa） Fragment：UNP residues 19-224
Chain J 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-Hcl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 1.98 Å R-free 0.236
3PVN Triclinic form of Human C-Reactive Protein in complex with Zinc Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain K 19–224（206 aa） Fragment：UNP residues 19-224
Chain L 19–224（206 aa） Fragment：UNP residues 19-224
Chain M 19–224（206 aa） Fragment：UNP residues 19-224
Chain N 19–224（206 aa） Fragment：UNP residues 19-224
Chain O 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-Hcl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 1.98 Å R-free 0.236
3PVN Triclinic form of Human C-Reactive Protein in complex with Zinc Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain P 19–224（206 aa） Fragment：UNP residues 19-224
Chain Q 19–224（206 aa） Fragment：UNP residues 19-224
Chain R 19–224（206 aa） Fragment：UNP residues 19-224
Chain S 19–224（206 aa） Fragment：UNP residues 19-224
Chain T 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-Hcl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 1.98 Å R-free 0.236
3PVO Monoclinic form of Human C-Reactive Protein Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa） Fragment：UNP residues 19-224
Chain B 19–224（206 aa） Fragment：UNP residues 19-224
Chain C 19–224（206 aa） Fragment：UNP residues 19-224
Chain D 19–224（206 aa） Fragment：UNP residues 19-224
Chain E 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-HCl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 3.00 Å R-free 0.285
3PVO Monoclinic form of Human C-Reactive Protein Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa） Fragment：UNP residues 19-224
Chain G 19–224（206 aa） Fragment：UNP residues 19-224
Chain H 19–224（206 aa） Fragment：UNP residues 19-224
Chain I 19–224（206 aa） Fragment：UNP residues 19-224
Chain J 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-HCl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 3.00 Å R-free 0.285
3PVO Monoclinic form of Human C-Reactive Protein Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain K 19–224（206 aa） Fragment：UNP residues 19-224
Chain L 19–224（206 aa） Fragment：UNP residues 19-224
Chain M 19–224（206 aa） Fragment：UNP residues 19-224
Chain N 19–224（206 aa） Fragment：UNP residues 19-224
Chain O 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-HCl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 3.00 Å R-free 0.285
3PVO Monoclinic form of Human C-Reactive Protein Deposited 2010-12-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain P 19–224（206 aa） Fragment：UNP residues 19-224
Chain Q 19–224（206 aa） Fragment：UNP residues 19-224
Chain R 19–224（206 aa） Fragment：UNP residues 19-224
Chain S 19–224（206 aa） Fragment：UNP residues 19-224
Chain T 19–224（206 aa） Fragment：UNP residues 19-224
Not recorded CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；289 K；12% PEG 4000, 0.1M Tris-HCl, 0.2M MgCl2, 0.05M LiCl, pH 8.0, VAPOR DIFFUSION, temperature 289K
Resolution 3.00 Å R-free 0.285
7PK9 C-reactive protein decamer at pH 7.5 Deposited 2021-08-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7PKB C-reactive protein pentamer at pH 7.5 Deposited 2021-08-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7PKD C-reactive protein decamer at pH 7.5 with phosphocholine ligand Deposited 2021-08-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 PC PHOSPHOCHOLINE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7PKD C-reactive protein decamer at pH 7.5 with phosphocholine ligand Deposited 2021-08-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 PC PHOSPHOCHOLINE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7PKE C-reactive protein pentamer at pH 7.5 with phosphocholine ligand Deposited 2021-08-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 PC PHOSPHOCHOLINE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7PKF C-reactive protein decamer at pH 5 Deposited 2021-08-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7PKG C-reactive protein pentamer at pH 5 Deposited 2021-08-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded CA CALCIUM ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7PKH C-reactive protein decamer at pH 5 with phosphocholine ligand Deposited 2021-08-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded CA CALCIUM ION × 20 PC PHOSPHOCHOLINE × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
7TBA Pentraxin - ligand complex Deposited 2021-12-21 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded XQY [3-(dibutylamino)propyl]phosphonic acid × 5 CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100mM Tris pH 9.0, 10% PEG 4000, 50mM lithium chloride, 200mM magnesium chloride
Resolution 3.50 Å R-free 0.260
7TBA Pentraxin - ligand complex Deposited 2021-12-21 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain F 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Chain I 19–224（206 aa）
Chain J 19–224（206 aa）
Not recorded XQY [3-(dibutylamino)propyl]phosphonic acid × 5 CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100mM Tris pH 9.0, 10% PEG 4000, 50mM lithium chloride, 200mM magnesium chloride
Resolution 3.50 Å R-free 0.260
7TBA Pentraxin - ligand complex Deposited 2021-12-21 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain K 19–224（206 aa）
Chain L 19–224（206 aa）
Chain M 19–224（206 aa）
Chain N 19–224（206 aa）
Chain O 19–224（206 aa）
Not recorded XQY [3-(dibutylamino)propyl]phosphonic acid × 5 CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100mM Tris pH 9.0, 10% PEG 4000, 50mM lithium chloride, 200mM magnesium chloride
Resolution 3.50 Å R-free 0.260
7TBA Pentraxin - ligand complex Deposited 2021-12-21 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain P 19–224（206 aa）
Chain Q 19–224（206 aa）
Chain R 19–224（206 aa）
Chain S 19–224（206 aa）
Chain T 19–224（206 aa）
Not recorded XQY [3-(dibutylamino)propyl]phosphonic acid × 5 CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100mM Tris pH 9.0, 10% PEG 4000, 50mM lithium chloride, 200mM magnesium chloride
Resolution 3.50 Å R-free 0.260
8WV4 C-reactive protein, pentamer Deposited 2023-10-23 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–224（224 aa）
Chain B 1–224（224 aa）
Chain C 1–224（224 aa）
Chain D 1–224（224 aa）
Chain E 1–224（224 aa）
Not recorded CA CALCIUM ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Blot force, 0
Resolution 3.30 Å
8WV5 C-reactive protein, decamer Deposited 2023-10-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 1–224（224 aa）
Chain B 1–224（224 aa）
Chain C 1–224（224 aa）
Chain D 1–224（224 aa）
Chain E 1–224（224 aa）
Chain F 1–224（224 aa）
Chain G 1–224（224 aa）
Chain H 1–224（224 aa）
Chain I 1–224（224 aa）
Chain J 1–224（224 aa）
Not recorded CA CALCIUM ION × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Blot force, 0
Resolution 3.50 Å
9JNY C recatived protein pentamer Deposited 2024-09-24 Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain E 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20mM Tris-HCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.74 Å
9JO7 CRP-HCAb4 complex Deposited 2024-09-24 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain B 19–224（206 aa）
Chain D 19–224（206 aa）
Chain F 19–224（206 aa）
Chain H 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20mM Tris-HCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.68 Å
9JO9 CRP-HCAb3 complex Deposited 2024-09-24 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 19–224（206 aa）
Chain D 19–224（206 aa）
Chain F 19–224（206 aa）
Chain H 19–224（206 aa）
Chain J 19–224（206 aa）
Chain L 19–224（206 aa）
Chain N 19–224（206 aa）
Chain Q 19–224（206 aa）
Chain S 19–224（206 aa）
Chain T 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20mM Tris-HCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.65 Å
9K94 CRP-HCAb2 complex Deposited 2024-10-25 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain C 19–224（206 aa）
Chain D 19–224（206 aa）
Chain F 19–224（206 aa）
Chain I 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20 mM Tris-HCL
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.04 Å
9KMP CRP-HCAb1 complex Deposited 2024-11-16 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain C 19–224（206 aa）
Chain E 19–224（206 aa）
Chain G 19–224（206 aa）
Chain H 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20mM Tris-HCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
9KMS CRP antigen-antibody2 complex Deposited 2024-11-17 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 19–224（206 aa）
Chain C 19–224（206 aa）
Chain E 19–224（206 aa）
Chain G 19–224（206 aa）
Chain I 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20mM Tris-HCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
9U4E Cryo-EM structure of the human CRP-CPS23F complex Deposited 2025-03-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–224（224 aa）
Chain B 1–224（224 aa）
Chain C 1–224（224 aa）
Chain D 1–224（224 aa）
Chain E 1–224（224 aa）
Not recorded CA CALCIUM ION × 10 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.78 Å
9VCA Binding site between C-reactive protein and c2cc monoclonal antibody Deposited 2025-06-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 19–224（206 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；20 mM Tris-HCl buffer (pH 7.6), containing 150 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.40 Å

23 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–206； UniProt 19–224 Author chain B； PDBConstruct 1–206； UniProt 19–224 Author chain C； PDBConstruct 1–206； UniProt 19–224 Author chain D； PDBConstruct 1–206； UniProt 19–224 Author chain E； PDBConstruct 1–206； UniProt 19–224 Author chain F； PDBConstruct 1–206； UniProt 19–224 Author chain G； PDBConstruct 1–206； UniProt 19–224 Author chain H； PDBConstruct 1–206； UniProt 19–224 Author chain I； PDBConstruct 1–206； UniProt 19–224 Author chain J； PDBConstruct 1–206； UniProt 19–224

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1lj7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lj7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lj7
Deposition date deposition_date2002-04-19
Structure title titleCrystal structure of calcium-depleted human C-reactive protein from perfectly twinned data
Keywords keywordspentraxin fold, pentamer, decamer, twinned, unknown function; UNKNOWN FUNCTION
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.11 Å
Radius of gyration Rg (electron density) rg_electron40.03 Å
Forward intensity I(0) i0691091000.00
Molecular weight molecular_weight225740.0 kDa
Excluded volume excluded_volume286320 ų
Envelope volume envelope_volume394450 ų
Hydration-shell volume shell_volume79409 ų
Envelope diameter envelope_diameter120.9 Å
Shell Rg shell_rg48.67 Å
Envelope Rg envelope_rg38.01 Å
Shape Rg shape_rg39.99 Å
Total Rg total_rg40.66 Å
Total atoms total_atoms15986
Residues n_residues2015
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax119.2 Å
Rg (real space) rg_real40.77 Å
Rg uncertainty (real space) rg_real_error0.66 Å
I(0) (real space) i0_real6.9110e+08
I(0) uncertainty (real space) i0_real_error1.0840e+07
Rg (reciprocal space) rg_reciprocal41.11 Å
I(0) (reciprocal space) i0_reciprocal691300000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.6 Å
Skewness Skewness skewness-0.142
Kurtosis Kurtosis kurtosis-0.564
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha142400000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.921
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd1lj7a_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7b_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7c_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7d_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7e_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7f_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7g_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7h_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7i_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)
Domain ID domain_idd1lj7j_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.5 — Pentraxin (pentaxin)

CATH v4.4 (10 domains)

Domain ID domain_id1lj7A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7E00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7F00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7G00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7H00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7I00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id1lj7J00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
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8. Citations (1)

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9. Files and Curves (10)