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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

Method: X-RAY DIFFRACTION Dmax: 130.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

prostatic acid phosphatase

OrganismNot specified

UniProt P15309

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 × 3 其他Polymer 4 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 33–386 Chain B； UniProt 33–386 Chain C； UniProt 33–386 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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
2 Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 33–386 Chain D； UniProt 33–386 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 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

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 1ND5 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 construct Different mutation/modification 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 construct 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 construct 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
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 oligomeric state Different ligand/ion 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 ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 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 × 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
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 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 × 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
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11 Different construct Different mutation/modification 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 33–374（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 × 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
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 22 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 1–354； UniProt 33–386 Author chain B； PDBConstruct 1–354； UniProt 33–386 Author chain C； PDBConstruct 1–354； UniProt 33–386 Author chain D； PDBConstruct 1–354； UniProt 33–386

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 1nd5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nd5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nd5
Deposition date deposition_date2002-12-07
Structure title titleCrystal 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
Keywords keywordsAcid Phosphatase, PAP, Prostate, Phosphate, inhibitor, HYDROLASE; HYDROLASE
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_guinier37.63 Å
Radius of gyration Rg (electron density) rg_electron37.32 Å
Forward intensity I(0) i0386764000.00
Molecular weight molecular_weight164630.0 kDa
Excluded volume excluded_volume207750 ų
Envelope volume envelope_volume255780 ų
Hydration-shell volume shell_volume57408 ų
Envelope diameter envelope_diameter142.3 Å
Shell Rg shell_rg43.13 Å
Envelope Rg envelope_rg37.11 Å
Shape Rg shape_rg37.31 Å
Total Rg total_rg37.70 Å
Total atoms total_atoms11592
Residues n_residues1368
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 dmax130.8 Å
Rg (real space) rg_real37.68 Å
Rg uncertainty (real space) rg_real_error0.84 Å
I(0) (real space) i0_real3.8680e+08
I(0) uncertainty (real space) i0_real_error5.0540e+06
Rg (reciprocal space) rg_reciprocal37.65 Å
I(0) (reciprocal space) i0_reciprocal386800000.0000
Solution quality estimate total_estimate0.8699
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.6 Å
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.2100 Å−1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha116100000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.783; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.956
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1nd5a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.2 — Histidine acid phosphatase
Domain ID domain_idd1nd5b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.2 — Histidine acid phosphatase
Domain ID domain_idd1nd5c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.2 — Histidine acid phosphatase
Domain ID domain_idd1nd5d_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.2 — Histidine acid phosphatase

CATH v4.4 (4 domains)

Domain ID domain_id1nd5A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id1nd5B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id1nd5C00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id1nd5D00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
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8. Citations (1)

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9. Files and Curves (10)