SAXSdb — 1jl0

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

S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	1,4-DIAMINOBUTANE × 2 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DCAM_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–334； UniProt 1–334 Author chain B； PDBConstruct 1–334； UniProt 1–334

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	1jl0
Deposition date deposition_date	2001-07-13
Structure title title	Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant
Keywords keywords	;SPERMIDINE BIOSYNTHESIS, LYASE, DECARBOXYLASE, PYRUVATE, S-ADENOSYLMETHIONINE, SANDWICH, ALLOSTERIC ENZYME, PYRUVOYL, ESTER INTERMEDIATE, HYDROXYALANINE ;; LYASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1jl0__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1jl0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1jl0__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.09 Å
Rg (electron density)	27.22 Å
Total Rg	28.07 Å
Atom count	5049
Residues	621
Excluded volume	90354 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1jl0__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME
Molecular weight formula_weight	38298.4 kDa
EC 编号 ec_number	4.1.1.50
Mutation mutation	H243A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6339

MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIAITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1,4-DIAMINOBUTANE
Molecular weight formula_weight	88.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Molecular weight formula_weight	122.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	806

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1jl0a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.156 — S-adenosylmethionine decarboxylase
Superfamily Superfamily superfamily	d.156.1 — S-adenosylmethionine decarboxylase
Family Family family	d.156.1.1 — S-adenosylmethionine decarboxylase

Domain ID domain_id	d1jl0b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.156 — S-adenosylmethionine decarboxylase
Superfamily Superfamily superfamily	d.156.1 — S-adenosylmethionine decarboxylase
Family Family family	d.156.1.1 — S-adenosylmethionine decarboxylase

CATH v4.4 (2 domains)

Domain ID domain_id	1jl0A00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	90 — S-adenosylmethionine decarboxylase
Homologous superfamily homologous superfamily	10 — S-adenosylmethionine decarboxylase

Domain ID domain_id	1jl0B00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	90 — S-adenosylmethionine decarboxylase
Homologous superfamily homologous superfamily	10 — S-adenosylmethionine decarboxylase

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Unit-cell length a length_a	74.760 Å
Unit-cell length b length_b	55.990 Å
Unit-cell length c length_c	90.210 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	109.72 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	19.910 Å
R factor r_factor	0.2210
R_work r_work	0.2150
R_free r_free	0.2370

Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant

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

S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1jl0__assembly_1__model_1

1jl0__assembly_1__model_1 | I(q)

1jl0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant

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

S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1jl0__assembly_1__model_1

1jl0__assembly_1__model_1 | I(q)

1jl0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)