9c2t

Infectious B19V capsid

Method: ELECTRON MICROSCOPY D_max: 214.1 Å Quality: GOOD

▼

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

Capsid protein 2

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain A； UniProt 2–554 Chain B； UniProt 2–554 Chain C； UniProt 2–554 Chain D； UniProt 2–554 Chain E； UniProt 2–554 Chain F； UniProt 2–554	Not recorded	Alpha-1-antichymotrypsin His-Pro-less × 1 （P01011）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.10 Å

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 9C2T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9C27 Infectious B19V capsid Deposited 2024-05-30	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.20 Å
9C27 Infectious B19V capsid Deposited 2024-05-30	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.20 Å
9C27 Infectious B19V capsid Deposited 2024-05-30	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.20 Å
9C27 Infectious B19V capsid Deposited 2024-05-30	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.20 Å
9C27 Infectious B19V capsid Deposited 2024-05-30	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.20 Å
9C4F Infectious B19V capsid Deposited 2024-06-04	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–554（554 aa） Chain B 1–554（554 aa） Chain C 1–554（554 aa） Chain D 1–554（554 aa） Chain E 1–554（554 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å

2 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q784T0_PAVHB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–553； UniProt 2–554 Author chain B； PDBConstruct 1–553； UniProt 2–554 Author chain C； PDBConstruct 1–553； UniProt 2–554 Author chain D； PDBConstruct 1–553； UniProt 2–554 Author chain E； PDBConstruct 1–553； UniProt 2–554 Author chain F； PDBConstruct 1–553； UniProt 2–554

Alpha-1-antichymotrypsin His-Pro-less

OrganismNot specified

UniProt P01011

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain S； UniProt 48–422	Not recorded	Capsid protein 2 × 6 （Q784T0）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.10 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9C2T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AS4 CLEAVED ANTICHYMOTRYPSIN A349R Deposited 1997-08-12	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 × 2 PDB declaration: dimeric	Chain A 43–383（341 aa） Fragment：CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393 Chain B 387–423（37 aa） Fragment：CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393	Mutation：A349R Mutation：A349R	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；14% PEG MONOMETHYLETHER 5000, 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM ACETATE PH 5.6 PROTEIN AT 3 MG/ML	Resolution 2.10 Å R-free 0.240
1QMN Alpha1-antichymotrypsin serpin in the delta conformation (partial loop insertion) Deposited 1999-10-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–423（398 aa）	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；1 MICROLITER OF 10MG/ML PROTEIN IN 50MM TRIS, 50MM KCL, PH 7.4 WAS MIXED WITH 2 MICROLITER OF PRECIPITANT AND EQUILIBRATED AS A HANGING DROP OVER 1ML OF PRECIPITANT (20% [W/V] PEG 4000, 0.2M AMMONIUM SULPHATE, 0.1M NAOAC, PH 4.5), AT 18 DEGREES C	Resolution 2.27 Å R-free 0.243
2ACH CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS Deposited 1993-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–383（360 aa） Chain B 384–423（40 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å
2ACH CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS Deposited 1993-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 24–383（360 aa） Chain B 384–423（40 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å
3CAA CLEAVED ANTICHYMOTRYPSIN A347R Deposited 1997-08-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 43–383（341 aa） Chain B 387–423（37 aa）	Mutation：A347R Mutation：A347R	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；10% PEG MONOMETHYLETHER 5000 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM CITRATE PH 5.6 PROTEIN AT 3 MG/ML	Resolution 2.40 Å R-free 0.280
3DLW Antichymotrypsin Deposited 2008-06-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–423（399 aa）	Mutation：A351G, A352T, V370T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；PEG 10,000, HEPES buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.286
4CAA CLEAVED ANTICHYMOTRYPSIN T345R Deposited 1997-08-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 43–383（341 aa） Chain B 387–423（37 aa）	Mutation：T345R Mutation：T345R	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；14% PEG 8000 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM CITRATE PH 5.6	Resolution 2.90 Å R-free 0.284
5OM2 Crystal structure of Alpha1-antichymotrypsin variant DBS-I1: a drug-binding serpin for doxycycline Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274A W276F R277F V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274A W276F R277F V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ;	EDO 1,2-ETHANEDIOL × 1 DXT (4S,4AR,5S,5AR,6R,12AS)-4-(DIMETHYLAMINO)-3,5,10,12,12A-PENTAHYDROXY-6-METHYL-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M ammonium chloride, 20 % w/v PEG 3350	Resolution 1.47 Å R-free 0.202
5OM3 Crystal structure of Alpha1-antichymotrypsin variant DBS-I5: a MMP14-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F V355L K356F T358P L360S S361L A362R L363M P382D T383H D384F Q386W N387S Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F V355L K356F T358P L360S S361L A362R L363M P382D T383H D384F Q386W N387S	PEG DI(HYDROXYETHYL)ETHER × 1 DXT (4S,4AR,5S,5AR,6R,12AS)-4-(DIMETHYLAMINO)-3,5,10,12,12A-PENTAHYDROXY-6-METHYL-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25 % w/v PEG 3350	Resolution 2.00 Å R-free 0.219
5OM5 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an allosterically triggered drug-binding serpin for doxycycline Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ;	EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 7.0, 30 % v/v Jeffamine ED-2001 pH 7.0	Resolution 1.59 Å R-free 0.196
5OM6 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2: a MMP9-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Fragment：UNP residues 36-383 Chain B 384–423（40 aa） Fragment：UNP residues 384-423	Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q	CIT CITRIC ACID × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M citric acid pH 3.5, 25 % w/v PEG 3350	Resolution 1.85 Å R-free 0.238
5OM6 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2: a MMP9-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 26–383（358 aa） Fragment：UNP residues 36-383 Chain D 384–423（40 aa） Fragment：UNP residues 384-423	Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q	CIT CITRIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M citric acid pH 3.5, 25 % w/v PEG 3350	Resolution 1.85 Å R-free 0.238
5OM7 Crystal structure of Alpha1-antichymotrypsin variant DBS-II: a drug-binding serpin for doxorubicin Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ;	DM2 DOXORUBICIN × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M ammonium chloride, 20 % w/v PEG 3350	Resolution 1.73 Å R-free 0.235
5OM8 Crystal form 2 of Alpha1-antichymotrypsin variant DBS-II-allo: an allosterically modulated drug-binding serpin for doxorubicin Deposited 2017-07-28	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; Mutation：;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ;	CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 1 NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Ammonium chloride, 20% w/v PEG 3350	Resolution 2.20 Å R-free 0.242
6FTP Crystal form 1 of Alpha1-antichymotrypsin variant DBS-II-allo: an allosterically modulated drug-binding serpin for doxorubicin Deposited 2018-02-22	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 386–423（38 aa）	Mutation：L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q Mutation：S361G A362P P382D T383N D384F Q386W N387S	EDO 1,2-ETHANEDIOL × 3 DM2 DOXORUBICIN × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M sodium thiocyanate, 20 % w/v PEG 3350	Resolution 1.80 Å R-free 0.221
6HGD Crystal structure of Alpha1-antichymotrypsin variant NewBG-0: a new binding globulin variant that is devoid of any cortisol-binding capabilities Deposited 2018-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, E242Q, K244N, K274N, R277G Mutation：P382D, T383H, D384F, Q386W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M magnesium chloride hexahydrate, 0.1 M BIS-Tris pH 6.5, 25 % w/v PEG 3350	Resolution 1.90 Å R-free 0.198
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–423（398 aa）	Mutation：L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8	Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 26–423（398 aa）	Mutation：L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8	Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 26–423（398 aa）	Mutation：L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8	Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 26–423（398 aa）	Mutation：L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8	Resolution 2.80 Å R-free 0.262
6HGF Crystal structure of Alpha1-antichymotrypsin variant NewBG-II: a new binding globulin in complex with cortisol Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, E242Q, K244N, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	EDO 1,2-ETHANEDIOL × 2 HCY (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium sulfate, 20 % w/v PEG 3350	Resolution 1.65 Å R-free 0.187
6HGG Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with cortisol Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	HCY (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione × 1 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350	Resolution 1.79 Å R-free 0.216
6HGH Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin without any bound ligand Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	MLA MALONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；4 % Tacsimate pH 4.0, 12 % w/v PEG 3350	Resolution 1.90 Å R-free 0.240
6HGI Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with corticosterone Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	C0R CORTICOSTERONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350	Resolution 1.52 Å R-free 0.193
6HGJ Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with aldosterone Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	AS4 ALDOSTERONE × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350	Resolution 1.82 Å R-free 0.221
6HGK Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with progesterone Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	STR PROGESTERONE × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2 % Tacsimate pH 6.0, 0.1 M BIS-Tris pH 6.5, 20 % w/v PEG 3350	Resolution 1.85 Å R-free 0.227
6HGL Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with testosterone Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation：P382D, T383H, D384F, Q386W, N387S	TES TESTOSTERONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350	Resolution 1.92 Å R-free 0.224
6HGM Crystal structure of Alpha1-antichymotrypsin variant NewBG-III-allo: an allosterically controlled new binding globulin with an unprecedentedly high ligand release efficacy Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G, A349R Mutation：P382D, T383H, D384F, Q386W, N387S	CL CHLORIDE ION × 3 CA CALCIUM ION × 3 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.3 M calcium chloride dihydrate, 20 % w/v PEG 3350	Resolution 1.37 Å R-free 0.181
6HGN Crystal structure of Alpha1-antichymotrypsin variant DBS-II-allo-L55V: an allosterically controlled doxorubicin-binding serpin with an unprecedentedly high ligand release efficacy Deposited 2018-08-23	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 × 2 PDB declaration: dimeric	Chain A 26–383（358 aa） Chain B 384–423（40 aa）	Mutation：L24R, L55V, W194F,W215Y, E242Q, K244N, L269S, P270Q, K274S, W276F, R277F, D278E, A349R, V355L, K356E, I357V, T358L, L359F, L360Q Mutation：S361G, A362P, P382D, T383N, D384F, Q386W, N387S	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2 % Tacsimate pH 4.0, 0.1 M Sodium acetate trihydrate pH 4.6, 16 % w/v PEG 3,350	Resolution 1.48 Å R-free 0.199
9D7K Infectious B19V capsid Deposited 2024-08-16	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain S 1–423（423 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

25 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AACT_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain S； PDBConstruct 1–375； UniProt 48–422

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

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9c2t
Deposition date deposition_date	2024-05-31
Structure title title	Infectious B19V capsid
Keywords keywords	B19, Virion, Capsid, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	53.34 Å
Radius of gyration Rg (electron density) rg_electron	53.03 Å
Forward intensity I(0) i0	2036080000.00
Molecular weight molecular_weight	381740.0 kDa
Excluded volume excluded_volume	478410 Å³
Envelope volume envelope_volume	641310 Å³
Hydration-shell volume shell_volume	98832 Å³
Envelope diameter envelope_diameter	222.9 Å
Shell Rg shell_rg	56.70 Å
Envelope Rg envelope_rg	54.14 Å
Shape Rg shape_rg	53.00 Å
Total Rg total_rg	53.25 Å
Total atoms total_atoms	26970
Residues n_residues	3461
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

▼

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

Maximum dimension Dmax dmax	214.1 Å
Rg (real space) rg_real	53.48 Å
Rg uncertainty (real space) rg_real_error	3.48 Å
I(0) (real space) i0_real	2.0360e+09
I(0) uncertainty (real space) i0_real_error	4.4330e+07
Rg (reciprocal space) rg_reciprocal	53.22 Å
I(0) (reciprocal space) i0_reciprocal	2035000000.0000
Solution quality estimate total_estimate	0.8083
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	59.1 Å
Skewness Skewness skewness	0.470
Kurtosis Kurtosis kurtosis	-0.053
Angular range angular_range	— – 0.1450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	218200000.0000
Real-space data points n_real_points	30
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.527; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.933; Smooth: 0.991

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Capsid protein 2
Molecular weight formula_weight	60784.8 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	26970

TSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLCMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVTGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL

Entity 2 Entity 2 polymer

Description description	Alpha-1-antichymotrypsin His-Pro-less
Molecular weight formula_weight	42500.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S

GLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLSALVETRTIVRFNRPFLMIIVPTDTQNIFFMSKVTNPKQ

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.10 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	380278

fit	/app/data/saxs_computation/c2/9c2t/9c2t.fit
pddf	/app/data/pr_computation/c2/9c2t/9c2t.pr.out
profile	/app/data/saxs_computation/c2/9c2t/9c2t.dat

Infectious B19V capsid

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

Capsid protein 2

State in the Current Structure

Other States of the Same Protein in the Database

Alpha-1-antichymotrypsin His-Pro-less

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)