5l3s

Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY

Method: X-RAY DIFFRACTION D_max: 169.3 Å Quality: GOOD

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

Signal recognition particle 54 kDa protein

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–292	Not recorded	Signal recognition particle receptor FtsY × 1 （P27414） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 7 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–292	Not recorded	Signal recognition particle receptor FtsY × 1 （P27414） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1–292	Not recorded	Signal recognition particle receptor FtsY × 1 （P27414） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 1–292	Not recorded	Signal recognition particle receptor FtsY × 1 （P27414） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 5 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216

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 5L3S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1QZW Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；Ammonium sulphate, sodium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.10 Å R-free 0.387
1QZW Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain C 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；Ammonium sulphate, sodium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.10 Å R-free 0.387
1QZW Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain E 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；Ammonium sulphate, sodium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.10 Å R-free 0.387
1QZW Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain G 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；Ammonium sulphate, sodium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.10 Å R-free 0.387
1QZX Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 8000, litium sulphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.00 Å R-free 0.383
1QZX Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication Deposited 2003-09-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–432（432 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 8000, litium sulphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 4.00 Å R-free 0.383
3KL4 Recognition of a signal peptide by the signal recognition particle Deposited 2009-11-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–432（431 aa） Fragment：UNP residues 2-432	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；295 K；5-7 % PEG 4000, 100 mM Bis-Tris, 100 mM NaCl, 5-50 mM Mg(OAc)2, 2 % Polypropylene glycol P400. Crystals were obtained by seeding, pH 5.5, VAPOR DIFFUSION, temperature 295K	Resolution 3.50 Å R-free 0.322
3ZN8 Structural Basis of Signal Sequence Surveillance and Selection by the SRP-SR Complex Deposited 2013-02-13	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: pentameric	Chain M 307–431（125 aa） Fragment：M, RESIDUES 327-431	Not recorded	MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer 50 MM HEPES-KOH, 100 MM KOAC, 8 MM MG(OAC)2, PH 7.5；pH 7.5；50 MM HEPES-KOH, 100 MM KOAC, 8 MM MG(OAC)2, PH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN；THE GRIDS WERE PLUNGE FROZEN IN LIQUID ETHANE USING A FEI MARK IV VITRIFICATION ROBOT AFTER BLOTTING FOR 1 S AT RT AND 100 PER CENT RELATIVE HUMIDITY	Resolution 12.00 Å
5L3V Structure of the crenarchaeal SRP54 GTPase bound to GDP Deposited 2016-05-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–293（293 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M CHES pH 6.0, 15 % (w/v) PEG 8000, 0.2 M ammonium sulfate	Resolution 2.30 Å R-free 0.222
5L3V Structure of the crenarchaeal SRP54 GTPase bound to GDP Deposited 2016-05-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–293（293 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M CHES pH 6.0, 15 % (w/v) PEG 8000, 0.2 M ammonium sulfate	Resolution 2.30 Å R-free 0.222

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SRP54_SULSO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 7–298； UniProt 1–292 Author chain C； PDBConstruct 7–298； UniProt 1–292 Author chain E； PDBConstruct 7–298； UniProt 1–292 Author chain G； PDBConstruct 7–298； UniProt 1–292

Signal recognition particle receptor FtsY

Sulfolobus acidocaldarius

UniProt P27414

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 79–368	Not recorded	Signal recognition particle 54 kDa protein × 1 （Q97ZE7） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 7 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 79–368	Not recorded	Signal recognition particle 54 kDa protein × 1 （Q97ZE7） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 79–368	Not recorded	Signal recognition particle 54 kDa protein × 1 （Q97ZE7） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 79–368	Not recorded	Signal recognition particle 54 kDa protein × 1 （Q97ZE7） GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GOL GLYCEROL × 5 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MES pH 5.8, 1.26 M ammonium sulfate	Resolution 1.90 Å R-free 0.216

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	FTSY_SULAC
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 7–296； UniProt 79–368 Author chain D； PDBConstruct 7–296； UniProt 79–368 Author chain F； PDBConstruct 7–296； UniProt 79–368 Author chain H； PDBConstruct 7–296； UniProt 79–368

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

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5l3s
Deposition date deposition_date	2016-05-24
Structure title title	Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY
Keywords keywords	Co-translational protein targeting, Signal Recognition Particle, GTPase, protein transport; PROTEIN TRANSPORT
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	48.70 Å
Radius of gyration Rg (electron density) rg_electron	49.01 Å
Forward intensity I(0) i0	887351000.00
Molecular weight molecular_weight	252970.0 kDa
Excluded volume excluded_volume	319030 Å³
Envelope volume envelope_volume	422070 Å³
Hydration-shell volume shell_volume	70731 Å³
Envelope diameter envelope_diameter	183.3 Å
Shell Rg shell_rg	52.96 Å
Envelope Rg envelope_rg	49.31 Å
Shape Rg shape_rg	49.02 Å
Total Rg total_rg	49.11 Å
Total atoms total_atoms	17761
Residues n_residues	2207
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	169.3 Å
Rg (real space) rg_real	48.74 Å
Rg uncertainty (real space) rg_real_error	1.79 Å
I(0) (real space) i0_real	8.8740e+08
I(0) uncertainty (real space) i0_real_error	1.7440e+07
Rg (reciprocal space) rg_reciprocal	48.71 Å
I(0) (reciprocal space) i0_reciprocal	887300000.0000
Solution quality estimate total_estimate	0.8778
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	58.2 Å
Skewness Skewness skewness	0.254
Kurtosis Kurtosis kurtosis	-0.524
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	80550000.0000
Real-space data points n_real_points	33
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.925

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	Signal recognition particle 54 kDa protein
Molecular weight formula_weight	33113.2 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	19033

HHHHHHMLENIRDAVRKFLTGSTPYEKAVDEFIKDLQKSLISSDVNVKLVFSLTAKIKERLNKEKPPSVLERKEWFISIVYDELSKLFGGDKEPNVNPTKLPFIIMLVGVQGSGKTTTAGKLAYFYKKRGYKVGLVAADVYRPAAYDQLLQLGNQIGVQVYGEPNNQNPIEIAKKGVDIFVKNKMDIIIVDTAGRHGYGEETKLLEEMKEMYDVLKPDDVILVIDASIGQKAYDLASRFHQASPIGSVIITKMDGTAKGGGALSAVVATGATIKFIGTGEKIDELETFNAKRFVSRIL

来源 Source

来源生物 organism	Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
NCBI Class编号 ncbi_taxonomy_id	273057
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Signal recognition particle receptor FtsY
Molecular weight formula_weight	33440.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H

HHHHHHRSFFDFLKYKTIKEDDLNDVIEELRFQLLDSDVSYEVTEKILEDLKNNLIGKKVSRREEVEEIVINTLKKSITEILTKNQKTDLIEKIRSSGKKPFVIIFFGVNGVGKTTTIAKVVNMLKKNNLSTIIAASDTFRAAAQEQLAYHASKLEVQLIRGKYGADPASVAFDAISFAKSRNIDVVLIDTAGRMHIDSDLVEELKKVLRIAKPDFRILILDSLAGSDALEQARHFENNVGYDAVILTKVDADAKGGIALSLAYELKKPVVYMGVGQNYDDLIPFSPDWFVERIFS

来源 Source

来源生物 organism	Sulfolobus acidocaldarius
NCBI Class编号 ncbi_taxonomy_id	330779
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
Molecular weight formula_weight	522.2 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 non-polymer

Description description	GUANOSINE-5'-MONOPHOSPHATE
Molecular weight formula_weight	363.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 7 Entity 7 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1214

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d5l3sa1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.13 — Domain of the SRP/SRP receptor G-proteins
Family Family family	a.24.13.0 — automated matches

Domain ID domain_id	d5l3sa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

Domain ID domain_id	d5l3sc1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.13 — Domain of the SRP/SRP receptor G-proteins
Family Family family	a.24.13.0 — automated matches

Domain ID domain_id	d5l3sc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

Domain ID domain_id	d5l3se1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.13 — Domain of the SRP/SRP receptor G-proteins
Family Family family	a.24.13.0 — automated matches

Domain ID domain_id	d5l3se2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

Domain ID domain_id	d5l3sg1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.13 — Domain of the SRP/SRP receptor G-proteins
Family Family family	a.24.13.0 — automated matches

Domain ID domain_id	d5l3sg2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

CATH v4.4 (8 domains)

Domain ID domain_id	5l3sA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sG02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	5l3sH01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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8. Citations (1)

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Unit-cell length a length_a	51.196 Å
Unit-cell length b length_b	199.672 Å
Unit-cell length c length_c	124.869 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.95 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	37.870 Å
R factor r_factor	0.1741
R_work r_work	0.1732
R_free r_free	0.2162

fit	/app/data/saxs_computation/l3/5l3s/5l3s.fit
pddf	/app/data/pr_computation/l3/5l3s/5l3s.pr.out
profile	/app/data/saxs_computation/l3/5l3s/5l3s.dat

Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY

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

Signal recognition particle 54 kDa protein

State in the Current Structure

Other States of the Same Protein in the Database

Signal recognition particle receptor FtsY

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)