SAXSdb — 1zbd

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

RABPHILIN-3A

Rattus norvegicus

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 19–217	Fragment：19-217 Mutation：Q81L Non-standard monomer：Yes (specific site not provided by mmCIF)	RABPHILIN-3A × 1 （P47709） MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0	Resolution 2.60 Å R-free 0.263
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 19–217	Fragment：19-217 Mutation：Q81L Non-standard monomer：Yes (specific site not provided by mmCIF)	RABPHILIN-3A × 2 （P47709） MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0	Resolution 2.60 Å R-free 0.263

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 1ZBD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3RAB GPPNHP-BOUND RAB3A AT 2.0 A RESOLUTION Deposited 1998-11-16	Different construct Different mutation/modification 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 18–186（169 aa） Fragment：GTPASE DOMAIN	Not recorded	MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；CRYSTALLIZATION CONDITIONS: 14%PEG-8000,50 MM NAMES, PH 6.5, 200 MM NACL	Resolution 2.00 Å R-free 0.237

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RAB3A_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–203； UniProt 19–217

RABPHILIN-3A

Rattus norvegicus

UniProt P47709

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 41–170	Fragment：40-170, EFFECTOR DOMAIN Mutation：C108S Non-standard monomer：Yes (specific site not provided by mmCIF)	RABPHILIN-3A × 1 （P63012） MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0	Resolution 2.60 Å R-free 0.263
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 41–170	Fragment：40-170, EFFECTOR DOMAIN Mutation：C108S Non-standard monomer：Yes (specific site not provided by mmCIF)	RABPHILIN-3A × 2 （P63012） MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0	Resolution 2.60 Å R-free 0.263

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 1ZBD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2CHD Crystal structure of the C2A domain of Rabphilin-3A Deposited 2006-03-14	Different construct Different mutation/modification 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 371–510（140 aa） Fragment：C2A DOMAIN, RESIDUES 371-510	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 25% PEG4000, 0.1M AMMONIUM SULPHATE, 0.1M SODIUM ACETATE, PH=4.6	Resolution 1.92 Å R-free 0.269
2CM5 crystal structure of the C2B domain of rabphilin Deposited 2006-05-04	Different construct Different mutation/modification 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 519–684（166 aa） Fragment：C2B DOMAIN AND LINKER, RESIDUES 519-684	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 0.1M HEPES PH 8.5,20 % PEG MME 2000 OR 20 % PEG 8000	Resolution 1.28 Å R-free 0.194
2CM6 crystal structure of the C2B domain of rabphilin3A Deposited 2006-05-04	Different construct Different mutation/modification 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 519–684（166 aa） Fragment：C2B DOMAIN AND LINKER, RESIDUES 519-684	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 0.1 M HEPES PH 7.6, 25 % PEG 8000, 200 MM CA	Resolution 1.85 Å R-free 0.268
2CM6 crystal structure of the C2B domain of rabphilin3A Deposited 2006-05-04	Different construct Different mutation/modification 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 519–684（166 aa） Fragment：C2B DOMAIN AND LINKER, RESIDUES 519-684	Not recorded	CA CALCIUM ION × 2 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 0.1 M HEPES PH 7.6, 25 % PEG 8000, 200 MM CA	Resolution 1.85 Å R-free 0.268
3RPB THE C2B-DOMAIN OF RABPHILIN: STRUCTURAL VARIATIONS IN A JANUS-FACED DOMAIN Deposited 1999-04-19	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 541–680（140 aa） Fragment：C2B DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.1；304.5 K；Ionic strength (raw mmCIF value) 150 mM NMR sample composition 95% WATER/5% D2O	Resolution not provided
4LT7 Crystal structure of the c2a domain of rabphilin-3a in complex with a calcium Deposited 2013-07-23	Different construct Different mutation/modification 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 378–510（133 aa） Fragment：C2 1 domain residues 378-510	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；293 K；10 mM CaCl2, 150mM NaCl, 25mM HEPES ph 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.50 Å R-free 0.289
4NP9 Structure of Rabphilin C2A domain bound to IP3 Deposited 2013-11-21	Different construct Different mutation/modification 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 378–510（133 aa） Fragment：C2 domain, UNP RESIDUES 378-510	Not recorded	I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；25-28% PEG 4K, 10-20mM Ammonium sulfate, 100mM HEPES pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.92 Å R-free 0.250
4NS0 The C2A domain of Rabphilin 3A in complex with PI(4,5)P2 Deposited 2013-11-27	Different construct Different mutation/modification 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 378–510（133 aa） Fragment：C2 domain, UNP RESIDUES 378-510	Not recorded	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；25mM Hepes, 20mM Ammonuim Sulphate, 25% PEG 4K, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.80 Å R-free 0.226
5LO8 The C2B domain of Rabphilin 3A in complex with PI(4,5)P2 Deposited 2016-08-08	Different construct Different mutation/modification 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 536–680（145 aa） Fragment：C2B domain, UNP Residues 536-680	Not recorded	CA CALCIUM ION × 2 GOL GLYCEROL × 4 SO4 SULFATE ION × 1 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；24% PEG3350 0.1M ammonium sulfate 50mM Tris pH 7.5	Resolution 2.50 Å R-free 0.265
5LO8 The C2B domain of Rabphilin 3A in complex with PI(4,5)P2 Deposited 2016-08-08	Different construct Different mutation/modification 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 536–680（145 aa） Fragment：C2B domain, UNP Residues 536-680	Not recorded	CA CALCIUM ION × 2 GOL GLYCEROL × 3 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；24% PEG3350 0.1M ammonium sulfate 50mM Tris pH 7.5	Resolution 2.50 Å R-free 0.265
5LOB Structure of the Ca2+-bound Rabphilin3A C2B- SNAP25 complex (C2 space group) Deposited 2016-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 536–680（145 aa） Chain B 536–680（145 aa） Chain C 536–680（145 aa）	Not recorded	CA CALCIUM ION × 6 SO4 SULFATE ION × 10 GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；30% PEG3350 0.35 M Ammonium sulfate 0.1 M Tris pH 8.5	Resolution 3.30 Å R-free 0.286
5LOW Structure of the Ca2+-bound Rabphilin 3A C2B domain SNAP25 complex (P21 space group) Deposited 2016-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 536–680（145 aa） Chain B 536–680（145 aa） Chain C 536–680（145 aa）	Not recorded	GOL GLYCEROL × 3 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% PEG3350 0.35 M Ammonium sulfate 0.1 M Tris (pH 8.5) al's oil	Resolution 2.80 Å R-free 0.269
5LOW Structure of the Ca2+-bound Rabphilin 3A C2B domain SNAP25 complex (P21 space group) Deposited 2016-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain H 536–680（145 aa） Chain I 536–680（145 aa） Chain J 536–680（145 aa）	Not recorded	GOL GLYCEROL × 4 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% PEG3350 0.35 M Ammonium sulfate 0.1 M Tris (pH 8.5) al's oil	Resolution 2.80 Å R-free 0.269

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RP3A_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 5–134； UniProt 41–170

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	1zbd
Deposition date deposition_date	1998-11-06
Structure title title	STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A
Keywords keywords	G PROTEIN, EFFECTOR, RABCDR, SYNAPTIC EXOCYTOSIS, RAB PROTEIN, RAB3A, RABPHILIN; G PROTEIN
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	24.06 Å
Radius of gyration Rg (electron density) rg_electron	23.19 Å
Forward intensity I(0) i0	24768800.00
Molecular weight molecular_weight	35888.0 kDa
Excluded volume excluded_volume	43845 Å³
Envelope volume envelope_volume	53609 Å³
Hydration-shell volume shell_volume	21005 Å³
Envelope diameter envelope_diameter	87.5 Å
Shell Rg shell_rg	28.03 Å
Envelope Rg envelope_rg	23.47 Å
Shape Rg shape_rg	23.06 Å
Total Rg total_rg	24.17 Å
Total atoms total_atoms	2464
Residues n_residues	290
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	83.9 Å
Rg (real space) rg_real	24.27 Å
Rg uncertainty (real space) rg_real_error	0.76 Å
I(0) (real space) i0_real	2.4770e+07
I(0) uncertainty (real space) i0_real_error	3.6990e+05
Rg (reciprocal space) rg_reciprocal	24.22 Å
I(0) (reciprocal space) i0_reciprocal	24770000.0000
Solution quality estimate total_estimate	0.8393
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.9 Å
Skewness Skewness skewness	0.575
Kurtosis Kurtosis kurtosis	-0.110
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3267000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.735; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.783; Smooth: 0.921

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	RABPHILIN-3A
Molecular weight formula_weight	23439.3 kDa
Mutation mutation	Q81L
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2524

GSHMFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGLERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQD

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	RABPHILIN-3A
Molecular weight formula_weight	15668.4 kDa
Mutation mutation	C108S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GSHMRKQEELTDEEKEIINRVIARAEKMETMEQERIGRLVDRLETMRKNVAGDGVNRCILCGEQLGMLGSASVVCEDCKKNVCTKCGVETSNNRPHPVWLCKICLEQREVWKRSGAWFFKGFPKQVLPQPMPIK

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GUANOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	46

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1zbda_
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.37.1.8 — G proteins

Domain ID domain_id	d1zbdb_
Class class	g — Small proteins
Fold Fold fold	g.50 — FYVE/PHD zinc finger
Superfamily Superfamily superfamily	g.50.1 — FYVE/PHD zinc finger
Family Family family	g.50.1.1 — FYVE, a phosphatidylinositol-3-phosphate binding domain

CATH v4.4 (2 domains)

Domain ID domain_id	1zbdA00
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	1zbdB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	40 — Herpes Virus-1
Homologous superfamily homologous superfamily	10 — Zinc/RING finger domain, C3HC4 (zinc finger)

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8. Citations (1)

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Unit-cell length a length_a	89.315 Å
Unit-cell length b length_b	95.619 Å
Unit-cell length c length_c	47.715 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.49 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	90.000 Å
R factor r_factor	0.2260
R_work r_work	0.2260
R_free r_free	0.2630

fit	/app/data/saxs_computation/zb/1zbd/1zbd.fit
pddf	/app/data/pr_computation/zb/1zbd/1zbd.pr.out
profile	/app/data/saxs_computation/zb/1zbd/1zbd.dat

STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A

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

RABPHILIN-3A

State in the Current Structure

Other States of the Same Protein in the Database

RABPHILIN-3A

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 (6)

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 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)