SAXSdb — 1paa

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

YEAST TRANSCRIPTION FACTOR ADR1

Saccharomyces cerevisiae

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 130–159	Not recorded	ZN ZINC ION × 1	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	Resolution not provided

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 1PAA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ARD STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING Deposited 1993-10-01	Different construct	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–130（29 aa）	Not recorded	ZN ZINC ION × 1	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1ARE STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING Deposited 1993-10-01	Different construct	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–130（29 aa）	Not recorded	ZN ZINC ION × 1	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1ARF STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING Deposited 1993-10-01	Different construct	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–130（29 aa）	Not recorded	ZN ZINC ION × 1	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2ADR ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES Deposited 1998-03-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–161（60 aa） Fragment：DNA-BINDING DOMAIN	Mutation：C140A	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 5.5；303 K	Resolution not provided
5A7U Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel. Deposited 2015-07-10	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 130–158（29 aa） Fragment：RESIDUES 130-158	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer 20 MM HEPES PH 7.2 , 50 MM KOAC, 5 MM MG OAC2, 0.03% DDM, 50 MICROM ZNCL2, 125 MM SUCROSE.；pH 7.2；20 MM HEPES PH 7.2 , 50 MM KOAC, 5 MM MG OAC2, 0.03% DDM, 50 MICROM ZNCL2, 125 MM SUCROSE. cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- FEI VITROBOT MARK IV,	Resolution 4.80 Å

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

View Construct and Data Evidence

UniProt name	ADR1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–30； UniProt 130–159

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	1paa
Deposition date deposition_date	1994-07-15
Structure title title	STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION
Keywords keywords	TRANSCRIPTION REGULATION; TRANSCRIPTION REGULATION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	8.72 Å
Radius of gyration Rg (electron density) rg_electron	8.84 Å
Forward intensity I(0) i0	20925900.00
Molecular weight molecular_weight	34804.0 kDa
Excluded volume excluded_volume	42650 Å³
Envelope volume envelope_volume	8020 Å³
Hydration-shell volume shell_volume	6923 Å³
Envelope diameter envelope_diameter	36.5 Å
Shell Rg shell_rg	15.48 Å
Envelope Rg envelope_rg	10.99 Å
Shape Rg shape_rg	8.84 Å
Total Rg total_rg	9.28 Å
Total atoms total_atoms	4470
Residues n_residues	300
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	32.6 Å
Rg (real space) rg_real	8.73 Å
Rg uncertainty (real space) rg_real_error	0.39 Å
I(0) (real space) i0_real	2.0930e+07
I(0) uncertainty (real space) i0_real_error	2.4190e+05
Rg (reciprocal space) rg_reciprocal	8.73 Å
I(0) (reciprocal space) i0_reciprocal	20930000.0000
Solution quality estimate total_estimate	0.8378
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	31.8 Å
Skewness Skewness skewness	0.263
Kurtosis Kurtosis kurtosis	-0.137
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7855.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.702; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1paaa_
Class class	g — Small proteins
Fold Fold fold	g.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamily	g.37.1 — beta-beta-alpha zinc fingers
Family Family family	g.37.1.1 — Classic zinc finger, C2H2

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8. Citations (2)

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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	1

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

Description description	YEAST TRANSCRIPTION FACTOR ADR1
Molecular weight formula_weight	3435.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4470

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932

STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION

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

YEAST TRANSCRIPTION FACTOR ADR1

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/pa/1paa/1paa.fit
pddf	/app/data/pr_computation/pa/1paa/1paa.pr.out
profile	/app/data/saxs_computation/pa/1paa/1paa.dat