SAXSdb — 1aut

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

ACTIVATED PROTEIN C

OrganismNot specified

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 212–461 Chain L； UniProt 84–197	Non-standard monomer：Yes (specific site not provided by mmCIF)	0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.7；0.1 M CITRATE, 20% ISOPROPANOL 2% PEG 20000 PH 4.7	Resolution 2.80 Å

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 1AUT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1LQV Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C. Deposited 2002-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 43–75（33 aa） Fragment：Protein C Gla domain	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222
1LQV Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C. Deposited 2002-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 43–75（33 aa） Fragment：Protein C Gla domain	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222
3F6U Crystal structure of human Activated Protein C (APC) complexed with PPACK Deposited 2008-11-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 212–451（240 aa） Fragment：UNP residues 212-451 Chain L 91–188（98 aa） Fragment：UNP residues 91-188	Not recorded	0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1 NA SODIUM ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.236
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 43–75（33 aa） Fragment：GLA domain (UNP residues 43-75)	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 43–75（33 aa） Fragment：GLA domain (UNP residues 43-75)	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
4DT7 Crystal structure of thrombin bound to the activation domain QEDQVDPRLIDGKMTRRGDS of protein C Deposited 2012-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 204–223（20 aa） Fragment：UNP residues 204-223	Not recorded	NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1 M Tris, pH 8.5, 0.2 M Na acetate, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.90 Å R-free 0.218
4DT7 Crystal structure of thrombin bound to the activation domain QEDQVDPRLIDGKMTRRGDS of protein C Deposited 2012-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 204–223（20 aa） Fragment：UNP residues 204-223	Not recorded	NA SODIUM ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1 M Tris, pH 8.5, 0.2 M Na acetate, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.90 Å R-free 0.218
6M3B hAPC-c25k23 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 212–461（250 aa） Chain D 43–197（155 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1% n-Octyl-beta-D-glucoside, 0.1M sodium citrate tribasic dehydrate pH 5.5, 22% (w/v) PEG 3350	Resolution 2.20 Å R-free 0.247
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 212–461（250 aa） Chain B 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 212–461（250 aa） Chain D 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 212–461（250 aa） Chain I 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
8JRU Cryo-EM structure of the glucagon receptor bound to beta-arrestin 1 in ligand-free state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 205–216（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	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	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8JRV Cryo-EM structure of the glucagon receptor bound to glucagon and beta-arrestin 1 Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 205–216（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	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	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9BVM Vitamin K-dependent gamma-carboxylase with protein C propeptide and glutamate-rich region and with vitamin K hydroquinone Deposited 2024-05-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 19–88（70 aa）	Not recorded	A1AVC vitamin K1 hydroquinone × 1 6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9MOT Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27	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 × 3 PDB declaration: trimeric	Chain D 212–451（240 aa）	Mutation：S360A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
9MOV Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27	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 × 4 PDB declaration: tetrameric	Chain C 43–188（146 aa） Chain D 212–451（240 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S360A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

11 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PRTC_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain C； PDBConstruct 1–250； UniProt 212–461 Author chain L； PDBConstruct 1–114； UniProt 84–197

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	1aut
Deposition date deposition_date	1996-06-08
Structure title title	Human activated protein C
Keywords keywords	SERINE PROTEINASE, PLASMA CALCIUM BINDING, GLYCOPROTEIN, HYDROLASE-HYDROLASE INHIBITOR complex, BLOOD CLOTTING; HYDROLASE/HYDROLASE INHIBITOR
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	23.08 Å
Radius of gyration Rg (electron density) rg_electron	22.45 Å
Forward intensity I(0) i0	42486000.00
Molecular weight molecular_weight	36041.0 kDa
Excluded volume excluded_volume	36974 Å³
Envelope volume envelope_volume	60063 Å³
Hydration-shell volume shell_volume	22820 Å³
Envelope diameter envelope_diameter	82.8 Å
Shell Rg shell_rg	28.79 Å
Envelope Rg envelope_rg	23.37 Å
Shape Rg shape_rg	22.53 Å
Total Rg total_rg	22.93 Å
Total atoms total_atoms	3256
Residues n_residues	337
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	80.8 Å
Rg (real space) rg_real	23.14 Å
Rg uncertainty (real space) rg_real_error	0.58 Å
I(0) (real space) i0_real	4.2490e+07
I(0) uncertainty (real space) i0_real_error	5.7540e+05
Rg (reciprocal space) rg_reciprocal	23.13 Å
I(0) (reciprocal space) i0_reciprocal	42490000.0000
Solution quality estimate total_estimate	0.6683
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.1 Å
Skewness Skewness skewness	0.441
Kurtosis Kurtosis kurtosis	-0.253
Angular range angular_range	— – 0.3450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6152000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.760; Stabil: 1.000; Sysdev: 0.171; Positv: 1.000; Valcen: 0.914; Smooth: 0.977

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ACTIVATED PROTEIN C
Molecular weight formula_weight	28091.1 kDa
EC 编号 ec_number	3.4.21.69
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C
Atom count atom_count	3694

LIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP

Entity 2 Entity 2 polymer

Description description	ACTIVATED PROTEIN C
Molecular weight formula_weight	12730.6 kDa
EC 编号 ec_number	3.4.21.69
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

SKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHL

Entity 3 Entity 3 non-polymer

Description description	D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide
Molecular weight formula_weight	454.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	146

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1autc_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

Domain ID domain_id	d1autl1
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.11 — EGF/Laminin
Family Family family	g.3.11.1 — EGF-type module

Domain ID domain_id	d1autl2
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.11 — EGF/Laminin
Family Family family	g.3.11.1 — EGF-type module

CATH v4.4 (4 domains)

Domain ID domain_id	1autC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1autC02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1autL01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	25 — Laminin
Homologous superfamily homologous superfamily	10 — Laminin

Domain ID domain_id	1autL02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	25 — Laminin
Homologous superfamily homologous superfamily	10 — Laminin

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8. Citations (1)

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Unit-cell length a length_a	57.060 Å
Unit-cell length b length_b	89.600 Å
Unit-cell length c length_c	101.230 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.1840
R_free r_free	—

fit	/app/data/saxs_computation/au/1aut/1aut.fit
pddf	/app/data/pr_computation/au/1aut/1aut.pr.out
profile	/app/data/saxs_computation/au/1aut/1aut.dat

Human activated protein C

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

ACTIVATED PROTEIN C

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)