1b09

HUMAN C-REACTIVE PROTEIN COMPLEXED WITH PHOSPHOCHOLINE

Method: X-RAY DIFFRACTION D_max: 111.2 Å Quality: EXCELLENT

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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (C-REACTIVE PROTEIN)

OrganismNot specified

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	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

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 1B09	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
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
1LJ7 Crystal structure of calcium-depleted human C-reactive protein from perfectly twinned data Deposited 2002-04-19	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	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 3.15 Å R-free 0.199
1LJ7 Crystal structure of calcium-depleted human C-reactive protein from perfectly twinned data Deposited 2002-04-19	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	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 3.15 Å R-free 0.199
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 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 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 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 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	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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 38 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

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1b09
Deposition date deposition_date	1998-11-18
Structure title title	HUMAN C-REACTIVE PROTEIN COMPLEXED WITH PHOSPHOCHOLINE
Keywords keywords	PENTRAXIN, ACUTE-PHASE REACTANT, PHOSPHOCHOLINE, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	37.06 Å
Radius of gyration Rg (electron density) rg_electron	36.09 Å
Forward intensity I(0) i0	191518000.00
Molecular weight molecular_weight	116540.0 kDa
Excluded volume excluded_volume	147450 Å³
Envelope volume envelope_volume	195820 Å³
Hydration-shell volume shell_volume	44214 Å³
Envelope diameter envelope_diameter	109.4 Å
Shell Rg shell_rg	44.07 Å
Envelope Rg envelope_rg	34.66 Å
Shape Rg shape_rg	36.03 Å
Total Rg total_rg	36.84 Å
Total atoms total_atoms	8225
Residues n_residues	1030
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	111.2 Å
Rg (real space) rg_real	36.87 Å
Rg uncertainty (real space) rg_real_error	0.85 Å
I(0) (real space) i0_real	1.9150e+08
I(0) uncertainty (real space) i0_real_error	3.2080e+06
Rg (reciprocal space) rg_reciprocal	36.99 Å
I(0) (reciprocal space) i0_reciprocal	191500000.0000
Solution quality estimate total_estimate	0.9061
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.0 Å
Skewness Skewness skewness	-0.009
Kurtosis Kurtosis kurtosis	-0.828
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	129900000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.967

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d1b09a_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d1b09b_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d1b09c_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d1b09d_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d1b09e_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

CATH v4.4 (5 domains)

Domain ID domain_id	1b09A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1b09B00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1b09C00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1b09D00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1b09E00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

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8. Citations (1)

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Unit-cell length a length_a	193.940 Å
Unit-cell length b length_b	193.940 Å
Unit-cell length c length_c	134.430 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	40

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1960
R_free r_free	0.2420

Description description	PROTEIN (C-REACTIVE PROTEIN)
Molecular weight formula_weight	23068.0 kDa
Source method src_method	nat
Copy count entity_count	5

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	8225

HUMAN C-REACTIVE PROTEIN COMPLEXED WITH PHOSPHOCHOLINE

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (C-REACTIVE PROTEIN)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	10

Description description	PHOSPHOCHOLINE
Molecular weight formula_weight	184.2 kDa
Source method src_method	syn
Copy count entity_count	5

fit	/app/data/saxs_computation/b0/1b09/1b09.fit
pddf	/app/data/pr_computation/b0/1b09/1b09.pr.out
profile	/app/data/saxs_computation/b0/1b09/1b09.dat