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1eb4

Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida

Method: X-RAY DIFFRACTION Dmax: 92.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

HISTIDINE AMMONIA-LYASE

PSEUDOMONAS PUTIDA

UniProt P21310

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 2–510 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.1；2.0 M (NH4)2 SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL USED AS CRYOPROTECTANT Resolution 2.00 Å R-free 0.232

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 1EB4 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B8F Histidine ammonia-lyase (HAL) from Pseudomonas putida Deposited 1999-01-31 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–510（509 aa）
Mutation：C273A Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；CRYSTALLIZED FROM 2.0 M (NH4)2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT pH 8.1. 20 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT
Resolution 2.10 Å R-free 0.263
1GK2 Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida Deposited 2001-08-07 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–510（509 aa）
Chain B 2–510（509 aa）
Chain C 2–510（509 aa）
Chain D 2–510（509 aa）
Mutation：YES Mutation：YES Mutation：YES Mutation：YES GOL GLYCEROL × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；CRYSTALLIZED FROM 2.0 M (NH4)2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT
Resolution 1.90 Å R-free 0.226
1GK3 Histidine Ammonia-Lyase (HAL) Mutant D145A from Pseudomonas putida Deposited 2001-08-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–510（509 aa）
Mutation：YES SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；CRYSTALLIZED FROM 2.0 M (NH4)2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT
Resolution 2.25 Å R-free 0.280
1GKJ Histidine Ammonia-Lyase (HAL) Mutant Y280F from Pseudomonas putida Deposited 2001-08-15 Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–510（509 aa）
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；CRYSTALLIZED FROM 2.0 M (NH4)2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT
Resolution 1.70 Å R-free 0.236
1GKM HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE Deposited 2001-08-16 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain B 2–510（509 aa）
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) CYS CYSTEINE × 4 SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；CRYSTALLIZED FROM 2.0 M (NH4) 2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 25 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT
Resolution 1.00 Å R-free 0.135

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HUTH_PSEPU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–507； UniProt 2–510

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 1eb4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1eb4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1eb4
Deposition date deposition_date2001-07-19
Structure title titleHistidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida
Keywords keywordsLYASE, AMMONIA-LYASE, HISTIDINE DEGRADATION; LYASE
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_guinier27.24 Å
Radius of gyration Rg (electron density) rg_electron26.61 Å
Forward intensity I(0) i048210000.00
Molecular weight molecular_weight53665.0 kDa
Excluded volume excluded_volume67128 ų
Envelope volume envelope_volume79288 ų
Hydration-shell volume shell_volume25968 ų
Envelope diameter envelope_diameter95.0 Å
Shell Rg shell_rg32.60 Å
Envelope Rg envelope_rg26.97 Å
Shape Rg shape_rg26.61 Å
Total Rg total_rg27.22 Å
Total atoms total_atoms3767
Residues n_residues506
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 dmax92.6 Å
Rg (real space) rg_real27.46 Å
Rg uncertainty (real space) rg_real_error0.82 Å
I(0) (real space) i0_real4.8210e+07
I(0) uncertainty (real space) i0_real_error7.1960e+05
Rg (reciprocal space) rg_reciprocal27.40 Å
I(0) (reciprocal space) i0_reciprocal48210000.0000
Solution quality estimate total_estimate0.8514
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.5 Å
Skewness Skewness skewness0.517
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.2900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10940000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.867; Smooth: 0.906
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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) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1eb4a_
Class classa — All alpha proteins
Fold Fold folda.127 — L-aspartase-like
Superfamily Superfamily superfamilya.127.1 — L-aspartase-like
Family Family familya.127.1.2 — HAL/PAL-like

CATH v4.4 (2 domains)

Domain ID domain_id1eb4A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (N-terminal domain)
Domain ID domain_id1eb4A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (Central domain)
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8. Citations (3)

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9. Files and Curves (10)