1g63

PEPTIDYL-CYSTEINE DECARBOXYLASE EPID

Method: X-RAY DIFFRACTION

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

EPIDERMIN MODIFYING ENZYME EPID

Staphylococcus epidermidis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 12	FLAVIN MONONUCLEOTIDE × 12 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EPID_STAEP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 1–181 Author chain B； PDBConstruct 1–181； UniProt 1–181 Author chain C； PDBConstruct 1–181； UniProt 1–181 Author chain D； PDBConstruct 1–181； UniProt 1–181 Author chain E； PDBConstruct 1–181； UniProt 1–181 Author chain F； PDBConstruct 1–181； UniProt 1–181 Author chain G； PDBConstruct 1–181； UniProt 1–181 Author chain H； PDBConstruct 1–181； UniProt 1–181 Author chain I； PDBConstruct 1–181； UniProt 1–181 Author chain J； PDBConstruct 1–181； UniProt 1–181 Author chain K； PDBConstruct 1–181； UniProt 1–181 Author chain L； PDBConstruct 1–181； UniProt 1–181

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	1g63
Deposition date deposition_date	2000-11-03
Structure title title	PEPTIDYL-CYSTEINE DECARBOXYLASE EPID
Keywords keywords	alpha, beta protein, Rossmann like fold, OXIDOREDUCTASE; OXIDOREDUCTASE
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.

1g63__assembly_1__model_1

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

Download this curve (.dat)

1g63__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1g63__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	39.55 Å
Rg (electron density)	38.32 Å
Total Rg	38.71 Å
Atom count	16344
Residues	1983
Excluded volume	294140 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1g63__assembly_1__model_1`	dodecameric （12）	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 (3)

Entity 1 Entity 1 polymer

Description description	EPIDERMIN MODIFYING ENZYME EPID
Molecular weight formula_weight	20845.0 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

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	16760

MYGKLLICATASINVININHYIVELKQHFDEVNILFSPSSKNFINTDVLKLFCDNLYDEIKDPLLNHINIVENHEYILVLPASANTINKIANGICDNLLTTVCLTGYQKLFIFPNMNIRMWGNPFLQKNIDLLKNNDVKVYSPDMNKSFEISSGRYKNNITMPNIENVLNFVLNNEKRPLD

Source Source

Source organism organism	Staphylococcus epidermidis
NCBI taxonomy ID ncbi_taxonomy_id	1282
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	FLAVIN MONONUCLEOTIDE
Molecular weight formula_weight	456.3 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	416

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6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d1g63a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63h_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63i_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63j_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63k_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

Domain ID domain_id	d1g63l_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.34 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Superfamily Superfamily superfamily	c.34.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Family Family family	c.34.1.1 — Homo-oligomeric flavin-containing Cys decarboxylases, HFCD

CATH v4.4 (12 domains)

Domain ID domain_id	1g63A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63E00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63F00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63G00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63H00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63I00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63J00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63K00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

Domain ID domain_id	1g63L00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1950 — Flavin prenyltransferase-like

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Unit-cell length a length_a	164.680 Å
Unit-cell length b length_b	110.030 Å
Unit-cell length c length_c	152.870 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.35 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	48

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

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	14.990 Å
R factor r_factor	0.2300
R_work r_work	0.2300
R_free r_free	0.2630

PEPTIDYL-CYSTEINE DECARBOXYLASE EPID

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

EPIDERMIN MODIFYING ENZYME EPID

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

1g63__assembly_1__model_1

1g63__assembly_1__model_1 | I(q)

1g63__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (2)

PEPTIDYL-CYSTEINE DECARBOXYLASE EPID

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

EPIDERMIN MODIFYING ENZYME EPID

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

1g63__assembly_1__model_1

1g63__assembly_1__model_1 | I(q)

1g63__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (2)