SAXSdb — 2hpa

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

PROTEIN (ACID PHOSPHATASE)

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	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 33–374 Chain B； UniProt 33–374	Not recorded	alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PT3 N-PROPYL-TARTRAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 10；pH 10	Resolution 2.90 Å R-free 0.308
2	Other combination Homooligomer Protein × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 33–374 Chain D； UniProt 33–374	Not recorded	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PT3 N-PROPYL-TARTRAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 10；pH 10	Resolution 2.90 Å R-free 0.308
3	Other combination Homooligomer Protein × 4 其他Polymer 3 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 33–374 Chain B； UniProt 33–374 Chain C； UniProt 33–374 Chain D； UniProt 33–374	Not recorded	alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PT3 N-PROPYL-TARTRAMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 10；pH 10	Resolution 2.90 Å R-free 0.308

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 2HPA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 33–374（342 aa） Chain B 33–374（342 aa） Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLY GLYCINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–374（342 aa） Chain B 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GLY GLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLY GLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1ND5 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 33–386（354 aa） Chain B 33–386（354 aa） Chain C 33–386（354 aa）	Not recorded	2BF ALPHA-BENZYL-AMINOBENZYL-PHOSPHONIC ACID × 3 1PE PENTAETHYLENE GLYCOL × 7 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.279
1ND5 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	2BF ALPHA-BENZYL-AMINOBENZYL-PHOSPHONIC ACID × 2 1PE PENTAETHYLENE GLYCOL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.279
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–386（354 aa） Chain B 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 2 1PE PENTAETHYLENE GLYCOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GLY GLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 2 1PE PENTAETHYLENE GLYCOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 33–386（354 aa） Chain B 33–386（354 aa） Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 4 1PE PENTAETHYLENE GLYCOL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLY GLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
2L3H NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248-286 Deposited 2010-09-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.3；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 2.5 mM PAP248-286-1, 120 mM sodium chloride-2, 20 mM sodium phosphate-3, 200 mM [U-99% 2H] SDS-4, 10 % [U-99% 2H] D2O-5, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L77 Solution NMR structure of PAP248-286 in 50% TFE Deposited 2010-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Pressure ambient NMR sample composition 1.2 mM PAP248-286-1; 20 mM sodium phosphate-2; 10 % [U-99% 2H] D2O-3; 50 % [U-99% 2H] TFE-4; trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2L79 Solution NMR structure of PAP248-286 in 30% TFE Deposited 2010-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Pressure ambient NMR sample composition 1.2 mM PAP248-286-1; 20 mM sodium phosphate-2; 10 % [U-99% 2H] D2O-3; 30 % [U-99% 2H] TFE-4; trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2MG0 PAP262-270 in SDS micelles Deposited 2013-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 262–270（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K NMR sample composition 300 uM protein_1-1, 50 mM [U-99% 2H] SDS-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3PPD GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in Semen-Derived Enhancer of Viral Infection Deposited 2010-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 260–265（6 aa） Fragment：Residue 260-265	Not recorded	ZN ZINC ION × 6 ACY ACETIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1M MES pH6.0, 0.2M Zn(OAc)2, 10%(w/v)PEG-8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.219
7ZZV Prostatic acid phosphatase (PAP) fragment (85-120) Deposited 2022-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 85–120（36 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 0.8 mM pap85_120, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8XJ4 Structure of prostatic acid phosphatase in human semen Deposited 2023-12-20	Different construct 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 31–377（347 aa） Chain B 31–377（347 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MAN alpha-D-mannopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.19 Å
9NMU TCR156 bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 7 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 17% PEG 3500	Resolution 2.10 Å R-free 0.227
9NMV TCR156 S32Halpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 20% PEG3500	Resolution 1.97 Å R-free 0.217
9NMW TCR156 S30Ealpha S32Qalpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 11 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Na2SO4, bis tris propane pH 7.5, 20% PEG 3350	Resolution 2.11 Å R-free 0.232
9NMX TCR156 S32Malpha variant bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	MLI MALONATE ION × 2 GOL GLYCEROL × 12 NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 17% PEG 3500	Resolution 2.19 Å R-free 0.229
9NMY TCR156 S32Qalpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 9 MLI MALONATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.3；295 K；0.2 M sodium malonat, 20% PEG 3350	Resolution 2.01 Å R-free 0.227
9YTD Designed antibody vAB66 targeting PAP-HLA A*02:01 Deposited 2025-10-20	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 × 6 PDB declaration: hexameric	Chain C 112–120（9 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PPAP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–342； UniProt 33–374 Author chain B； PDBConstruct 1–342； UniProt 33–374 Author chain C； PDBConstruct 1–342； UniProt 33–374 Author chain D； PDBConstruct 1–342； UniProt 33–374

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2hpa
Deposition date deposition_date	1998-09-11
Structure title title	STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE
Keywords keywords	ACID PHOSPHATASE, N-PROPYLTARTRAMATE, HYDROLASE; HYDROLASE
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	37.31 Å
Radius of gyration Rg (electron density) rg_electron	37.02 Å
Forward intensity I(0) i0	376795000.00
Molecular weight molecular_weight	162000.0 kDa
Excluded volume excluded_volume	204250 Å³
Envelope volume envelope_volume	250060 Å³
Hydration-shell volume shell_volume	56600 Å³
Envelope diameter envelope_diameter	139.7 Å
Shell Rg shell_rg	42.85 Å
Envelope Rg envelope_rg	36.84 Å
Shape Rg shape_rg	37.01 Å
Total Rg total_rg	37.42 Å
Total atoms total_atoms	11416
Residues n_residues	1368
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	129.7 Å
Rg (real space) rg_real	37.35 Å
Rg uncertainty (real space) rg_real_error	1.08 Å
I(0) (real space) i0_real	3.7680e+08
I(0) uncertainty (real space) i0_real_error	6.1180e+06
Rg (reciprocal space) rg_reciprocal	37.32 Å
I(0) (reciprocal space) i0_reciprocal	376800000.0000
Solution quality estimate total_estimate	0.8686
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	43.2 Å
Skewness Skewness skewness	0.422
Kurtosis Kurtosis kurtosis	-0.135
Angular range angular_range	— – 0.2100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	96880000.0000
Real-space data points n_real_points	43
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.781; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.946

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	PROTEIN (ACID PHOSPHATASE)
Molecular weight formula_weight	39776.4 kDa
EC 编号 ec_number	3.1.3.2
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	11766

KELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMT

Entity 2 Entity 2 branched

Description description	alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	545.5 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 branched

Description description	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	586.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	5

Entity 6 Entity 6 non-polymer

Description description	N-PROPYL-TARTRAMIC ACID
Molecular weight formula_weight	191.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	350

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2hpaa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamily	c.60.1 — Phosphoglycerate mutase-like
Family Family family	c.60.1.2 — Histidine acid phosphatase

Domain ID domain_id	d2hpab_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamily	c.60.1 — Phosphoglycerate mutase-like
Family Family family	c.60.1.2 — Histidine acid phosphatase

Domain ID domain_id	d2hpac_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamily	c.60.1 — Phosphoglycerate mutase-like
Family Family family	c.60.1.2 — Histidine acid phosphatase

Domain ID domain_id	d2hpad_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamily	c.60.1 — Phosphoglycerate mutase-like
Family Family family	c.60.1.2 — Histidine acid phosphatase

CATH v4.4 (4 domains)

Domain ID domain_id	2hpaA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1240 — Phosphoglycerate mutase-like

Domain ID domain_id	2hpaB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1240 — Phosphoglycerate mutase-like

Domain ID domain_id	2hpaC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1240 — Phosphoglycerate mutase-like

Domain ID domain_id	2hpaD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1240 — Phosphoglycerate mutase-like

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8. Citations (2)

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Unit-cell length a length_a	119.860 Å
Unit-cell length b length_b	202.680 Å
Unit-cell length c length_c	71.110 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	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2110
R_work r_work	0.2110
R_free r_free	0.3080

fit	/app/data/saxs_computation/hp/2hpa/2hpa.fit
pddf	/app/data/pr_computation/hp/2hpa/2hpa.pr.out
profile	/app/data/saxs_computation/hp/2hpa/2hpa.dat

STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE