SAXSdb — 1fp3

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

N-ACYL-D-GLUCOSAMINE 2-EPIMERASE

Sus scrofa

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RENBP_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–402； UniProt 1–402 Author chain B； PDBConstruct 1–402； UniProt 1–402

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	1fp3
Deposition date deposition_date	2000-08-30
Structure title title	CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY
Keywords keywords	ALPHA/ALPHA-BARREL, N-acyl-D-glucosamine 2-epimerase, ISOMERASE; ISOMERASE
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.

1fp3__assembly_1__model_1

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

Download this curve (.dat)

1fp3__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1fp3__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.39 Å
Rg (electron density)	28.61 Å
Total Rg	29.25 Å
Atom count	6530
Residues	804
Excluded volume	115310 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1fp3__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1fp3__assembly_2__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 (2)

Entity 1 Entity 1 polymer

Description description	N-ACYL-D-GLUCOSAMINE 2-EPIMERASE
Molecular weight formula_weight	46465.1 kDa
EC 编号 ec_number	5.1.3.8
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	6675

MEKERETLQAWKERVGQELDRVMAFWLEHSHDREHGGFFTCLGRDGRVYDDLKYVWLQGRQVWMYCRLYRKLERFHRPELLDAAKAGGEFLLRHARVAPPEKKCAFVLTRDGRPVKVQRSIFSECFYTMAMNELWRVTAEARYQSEAVDMMDQIVHWVREDPSGLGRPQLPGAVASESMAVPMMLLCLVEQLGEEDEELAGRYAQLGHWCARRILQHVQRDGQAVLENVSEDGEELSGCLGRHQNPGHALEAGWFLLRHSSRSGDAKLRAHVIDTFLLLPFRSGWDADHGGLFYFQDADGLCPTQLEWAMKLWWPHSEAMIAFLMGYSESGDPALLRLFYQVAEYTFRQFRDPEYGEWFGYLNREGKVALTIKGGPFKGCFHVPRCLAMCEEMLSALLSRLA

Source Source

Source organism organism	Sus scrofa
Common name common_name	pig
NCBI taxonomy ID ncbi_taxonomy_id	9823
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
EC 编号 ec_number	5.1.3.8
Source method src_method	nat
Copy count entity_count	145

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1fp3a_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.1 — Six-hairpin glycosidases
Family Family family	a.102.1.3 — N-acylglucosamine (NAG) epimerase

Domain ID domain_id	d1fp3b_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.1 — Six-hairpin glycosidases
Family Family family	a.102.1.3 — N-acylglucosamine (NAG) epimerase

CATH v4.4 (2 domains)

Domain ID domain_id	1fp3A00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1fp3B00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	10 —

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Unit-cell length a length_a	78.138 Å
Unit-cell length b length_b	97.193 Å
Unit-cell length c length_c	100.651 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	8

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	14.970 Å
R factor r_factor	0.1690
R_work r_work	0.1690
R_free r_free	0.2440

CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY

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

N-ACYL-D-GLUCOSAMINE 2-EPIMERASE

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

1fp3__assembly_1__model_1

1fp3__assembly_1__model_1 | I(q)

1fp3__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY

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

N-ACYL-D-GLUCOSAMINE 2-EPIMERASE

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

1fp3__assembly_1__model_1

1fp3__assembly_1__model_1 | I(q)

1fp3__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)