1s9c

Crystal structure analysis of the 2-enoyl-CoA hydratase 2 domain of human peroxisomal multifunctional enzyme type 2

Method: X-RAY DIFFRACTION D_max: 225.9 Å Quality: GOOD

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

Peroxisomal multifunctional enzyme type 2

Homo sapiens

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 A； UniProt 318–615 Chain B； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 318–615 Chain D； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 318–615 Chain F； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265
4	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 318–615 Chain H； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265
5	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 318–615 Chain J； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265
6	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain K； UniProt 318–615 Chain L； UniProt 318–615	Fragment：2-enoyl-coenzyme A hydratase 2 domain Mutation：S318M, T319A, I559V, T615L	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；PEG 10000, HEPES, MnCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.265

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 1S9C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1IKT LIGANDED STEROL CARRIER PROTEIN TYPE 2 (SCP-2) LIKE DOMAIN OF HUMAN MULTIFUNCTIONAL ENZYME TYPE 2 (MFE-2) Deposited 2001-05-07	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 618–736（119 aa） Fragment：C-terminal domain, Residues 618-736	Not recorded	SO4 SULFATE ION × 2 OXN OXTOXYNOL-10 × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；ammonium sulfate, sodium chloride, Triton X-100, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.75 Å R-free 0.214
1ZBQ Crystal Structure Of Human 17-Beta-Hydroxysteroid Dehydrogenase Type 4 In Complex With NAD Deposited 2005-04-08	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 A 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN Chain B 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.2M Lithium Sulphate monohydrate, 0.1M TRIS hydrochloride pH8.5, 30% w/v polyethylene glycol 4000, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.19 Å R-free 0.236
1ZBQ Crystal Structure Of Human 17-Beta-Hydroxysteroid Dehydrogenase Type 4 In Complex With NAD Deposited 2005-04-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN Chain D 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.2M Lithium Sulphate monohydrate, 0.1M TRIS hydrochloride pH8.5, 30% w/v polyethylene glycol 4000, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.19 Å R-free 0.236
1ZBQ Crystal Structure Of Human 17-Beta-Hydroxysteroid Dehydrogenase Type 4 In Complex With NAD Deposited 2005-04-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN Chain F 1–304（304 aa） Fragment：N-terminal SHORT CHAIN DEHYDROGENASE DOMAIN	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.2M Lithium Sulphate monohydrate, 0.1M TRIS hydrochloride pH8.5, 30% w/v polyethylene glycol 4000, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.19 Å R-free 0.236
6Z1W Crystal structure of human steroid carrier protein SL (SCP-2L) mutant A100C Deposited 2020-05-14	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 643–761（119 aa）	Mutation：A100C	OXN OXTOXYNOL-10 × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；277 K；2.2 M ammonium sulfate, 0.2 M NaCl and 0.1 M citric acid	Resolution 2.48 Å R-free 0.268
6Z1X Crystal structure of human steroid carrier protein SL (SCP-2L) mutant V83C Deposited 2020-05-14	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 643–761（119 aa）	Mutation：V83C	OXN OXTOXYNOL-10 × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；277 K；2.2 M ammonium sulfate, 0.2 M NaCl and 0.1 M citric acid	Resolution 2.09 Å R-free 0.237
8AF2 Human Sterol Carrier Protein with unnatural amino acid 2,2'-bipyridine alanine incorporated at position 111 Deposited 2022-07-15	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 618–736（119 aa）	Mutation：;2,2'-bipyridine alanine incorporated at position 111 ; Non-standard monomer：Yes (specific site not provided by mmCIF)	TRT FRAGMENT OF TRITON X-100 × 2 SO4 SULFATE ION × 1 CU COPPER (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；281 K；well solution 2.3M ammonium sulphate, 100 mM citric acid pH 5.6 and 200 mM NaCl	Resolution 2.51 Å R-free 0.300
8AF2 Human Sterol Carrier Protein with unnatural amino acid 2,2'-bipyridine alanine incorporated at position 111 Deposited 2022-07-15	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 618–736（119 aa）	Mutation：;2,2'-bipyridine alanine incorporated at position 111 ; Non-standard monomer：Yes (specific site not provided by mmCIF)	TRT FRAGMENT OF TRITON X-100 × 1 SO4 SULFATE ION × 1 CU COPPER (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；281 K；well solution 2.3M ammonium sulphate, 100 mM citric acid pH 5.6 and 200 mM NaCl	Resolution 2.51 Å R-free 0.300
8AF3 Sterol carrier protein Artifical metalloenzyme incorporating Q111C mutation coupled to 2,2'-bipyridine Deposited 2022-07-15	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 618–736（119 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	TRT FRAGMENT OF TRITON X-100 × 1 SO4 SULFATE ION × 2 CU COPPER (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；278 K；well solution 2.3M ammonium sulphate, 100 mM citric acid pH 5.6 and 200 mM NaCl	Resolution 1.52 Å R-free 0.239

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DHB4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–298； UniProt 318–615 Author chain B； PDBConstruct 1–298； UniProt 318–615 Author chain C； PDBConstruct 1–298； UniProt 318–615 Author chain D； PDBConstruct 1–298； UniProt 318–615 Author chain E； PDBConstruct 1–298； UniProt 318–615 Author chain F； PDBConstruct 1–298； UniProt 318–615 Author chain G； PDBConstruct 1–298； UniProt 318–615 Author chain H； PDBConstruct 1–298； UniProt 318–615 Author chain I； PDBConstruct 1–298； UniProt 318–615 Author chain J； PDBConstruct 1–298； UniProt 318–615 Author chain K； PDBConstruct 1–298； UniProt 318–615 Author chain L； PDBConstruct 1–298； UniProt 318–615

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	1s9c
Deposition date deposition_date	2004-02-04
Structure title title	Crystal structure analysis of the 2-enoyl-CoA hydratase 2 domain of human peroxisomal multifunctional enzyme type 2
Keywords keywords	HOT-DOG FOLD, HYDRATASE 2 MOTIF, MULTIFUNCTIONAL, LYASE; LYASE
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	65.54 Å
Radius of gyration Rg (electron density) rg_electron	66.62 Å
Forward intensity I(0) i0	1536210000.00
Molecular weight molecular_weight	344930.0 kDa
Excluded volume excluded_volume	437800 Å³
Envelope volume envelope_volume	675020 Å³
Hydration-shell volume shell_volume	90108 Å³
Envelope diameter envelope_diameter	238.6 Å
Shell Rg shell_rg	60.98 Å
Envelope Rg envelope_rg	64.74 Å
Shape Rg shape_rg	66.61 Å
Total Rg total_rg	66.54 Å
Total atoms total_atoms	24344
Residues n_residues	3128
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	225.9 Å
Rg (real space) rg_real	66.50 Å
Rg uncertainty (real space) rg_real_error	2.55 Å
I(0) (real space) i0_real	1.5360e+09
I(0) uncertainty (real space) i0_real_error	3.5880e+07
Rg (reciprocal space) rg_reciprocal	64.68 Å
I(0) (reciprocal space) i0_reciprocal	1531000000.0000
Solution quality estimate total_estimate	0.8157
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	65.9 Å
Skewness Skewness skewness	0.568
Kurtosis Kurtosis kurtosis	-0.227
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	47790000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.796; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.280

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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) 48 domains

SCOP 2.08 (24 domains)

Domain ID domain_id	d1s9ca1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ca2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cd1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cd2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ce1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ce2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cf1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cf2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cg1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cg2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ch1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ch2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ci1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ci2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cj1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cj2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ck1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9ck2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cl1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

Domain ID domain_id	d1s9cl2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.38 — Thioesterase/thiol ester dehydrase-isomerase
Superfamily Superfamily superfamily	d.38.1 — Thioesterase/thiol ester dehydrase-isomerase
Family Family family	d.38.1.4 — MaoC-like

CATH v4.4 (24 domains)

Domain ID domain_id	1s9cA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cC01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cC02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cD02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cE01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cE02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cF01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cF02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cG01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cG02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cH01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cH02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cI01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cI02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cJ01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cJ02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cK01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cK02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cL01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

Domain ID domain_id	1s9cL02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	129 — Thiol Ester Dehydrase; Chain A
Homologous superfamily homologous superfamily	10 — Hotdog Thioesterase

▶

8. Citations (1)

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Unit-cell length a length_a	98.295 Å
Unit-cell length b length_b	105.431 Å
Unit-cell length c length_c	206.944 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.37 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

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

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	—
R_work r_work	0.2285
R_free r_free	0.2646

Description description	Peroxisomal multifunctional enzyme type 2
Molecular weight formula_weight	32236.0 kDa
EC 编号 ec_number	4.2.1.-
Mutation mutation	S318M, T319A, I559V, T615L
Source method src_method	man
Copy count entity_count	12

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	24524

Crystal structure analysis of the 2-enoyl-CoA hydratase 2 domain of human peroxisomal multifunctional enzyme type 2

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

Peroxisomal multifunctional enzyme type 2

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 48 domains

SCOP 2.08 (24 domains)

CATH v4.4 (24 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	180

fit	/app/data/saxs_computation/s9/1s9c/1s9c.fit
pddf	/app/data/pr_computation/s9/1s9c/1s9c.pr.out
profile	/app/data/saxs_computation/s9/1s9c/1s9c.dat