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3l2y

The structure of C-reactive protein bound to phosphoethanolamine

Method: X-RAY DIFFRACTION Dmax: 225.6 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 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
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 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
3 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain K； UniProt 19–224 Chain L； UniProt 19–224 Chain M； UniProt 19–224 Chain N； UniProt 19–224 Chain O； UniProt 19–224 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
4 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain P； UniProt 19–224 Chain Q； UniProt 19–224 Chain R； UniProt 19–224 Chain S； UniProt 19–224 Chain T； UniProt 19–224 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

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 3L2Y 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
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
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 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 35 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 Author chain K； PDBConstruct 1–206； UniProt 19–224 Author chain L； PDBConstruct 1–206； UniProt 19–224 Author chain M； PDBConstruct 1–206； UniProt 19–224 Author chain N； PDBConstruct 1–206； UniProt 19–224 Author chain O； PDBConstruct 1–206； UniProt 19–224 Author chain P； PDBConstruct 1–206； UniProt 19–224 Author chain Q； PDBConstruct 1–206； UniProt 19–224 Author chain R； PDBConstruct 1–206； UniProt 19–224 Author chain S； PDBConstruct 1–206； UniProt 19–224 Author chain T； 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 3l2y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3l2y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3l2y
Deposition date deposition_date2009-12-15
Structure title titleThe structure of C-reactive protein bound to phosphoethanolamine
Keywords keywords;PENTRAXIN, ACUTE PHASE REACTANT, IMMUNE SYSTEM, PHOSPHOETHANOLAMINE, Acute phase, Metal-binding, Pyrrolidone carboxylic acid, Secreted, Calcium-BINDING PROTEIN ;; Calcium-BINDING PROTEIN
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_guinier63.91 Å
Radius of gyration Rg (electron density) rg_electron63.98 Å
Forward intensity I(0) i02810000000.00
Molecular weight molecular_weight465290.0 kDa
Excluded volume excluded_volume588070 ų
Envelope volume envelope_volume850600 ų
Hydration-shell volume shell_volume111910 ų
Envelope diameter envelope_diameter211.9 Å
Shell Rg shell_rg63.68 Å
Envelope Rg envelope_rg61.89 Å
Shape Rg shape_rg63.94 Å
Total Rg total_rg64.12 Å
Total atoms total_atoms32840
Residues n_residues4120
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 dmax225.6 Å
Rg (real space) rg_real64.20 Å
Rg uncertainty (real space) rg_real_error2.33 Å
I(0) (real space) i0_real2.8100e+09
I(0) uncertainty (real space) i0_real_error6.7490e+07
Rg (reciprocal space) rg_reciprocal63.61 Å
I(0) (reciprocal space) i0_reciprocal2807000000.0000
Solution quality estimate total_estimate0.8330
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.2 Å
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.585
Angular range angular_range— – 0.1250 Å−1
Current regularization parameter α current_alpha0.0012
Highest regularization parameter α highest_alpha272200000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.800
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (20 domains)

Domain ID domain_idd3l2ya_
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_idd3l2yb_
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_idd3l2yc_
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_idd3l2yd_
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_idd3l2ye_
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_idd3l2yf_
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_idd3l2yg_
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_idd3l2yh_
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_idd3l2yi_
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_idd3l2yj_
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_idd3l2yk_
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_idd3l2yl_
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_idd3l2ym_
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_idd3l2yn_
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_idd3l2yo_
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_idd3l2yp_
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_idd3l2yq_
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_idd3l2yr_
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_idd3l2ys_
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_idd3l2yt_
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 (20 domains)

Domain ID domain_id3l2yA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yG00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yI00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yJ00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yK00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yM00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yN00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yO00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yP00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yQ00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yR00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yS00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200 —
Domain ID domain_id3l2yT00
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)