SAXSdb — 2fkm

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

Phosphomannomutase/phosphoglucomutase

Pseudomonas aeruginosa

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	1,6-di-O-phosphono-alpha-D-glucopyranose × 1 ZINC ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ALGC_PSEAE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain X； PDBConstruct 1–462； UniProt 1–462

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	2fkm
Deposition date deposition_date	2006-01-04
Structure title title	PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound
Keywords keywords	alpha/beta protein, enzyme-metal complex, enzyme-ligand complex, 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.

2fkm__assembly_1__model_1

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

Download this curve (.dat)

2fkm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2fkm__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.51 Å
Rg (electron density)	21.52 Å
Total Rg	22.29 Å
Atom count	3396
Residues	454
Excluded volume	60399 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2fkm__assembly_1__model_1`	monomeric （1）	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	Phosphomannomutase/phosphoglucomutase
Molecular weight formula_weight	50247.2 kDa
EC 编号 ec_number	5.4.2.8
Mutation mutation	s108d
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X
Atom count atom_count	3638

STAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGDHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF

Source Source

Source organism organism	Pseudomonas aeruginosa
NCBI taxonomy ID ncbi_taxonomy_id	287
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	1,6-di-O-phosphono-alpha-D-glucopyranose
Molecular weight formula_weight	339.1 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 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	234

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2fkmx1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.84 — Phosphoglucomutase, first 3 domains
Superfamily Superfamily superfamily	c.84.1 — Phosphoglucomutase, first 3 domains
Family Family family	c.84.1.1 — Phosphoglucomutase, first 3 domains

Domain ID domain_id	d2fkmx2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.84 — Phosphoglucomutase, first 3 domains
Superfamily Superfamily superfamily	c.84.1 — Phosphoglucomutase, first 3 domains
Family Family family	c.84.1.1 — Phosphoglucomutase, first 3 domains

Domain ID domain_id	d2fkmx3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.84 — Phosphoglucomutase, first 3 domains
Superfamily Superfamily superfamily	c.84.1 — Phosphoglucomutase, first 3 domains
Family Family family	c.84.1.1 — Phosphoglucomutase, first 3 domains

Domain ID domain_id	d2fkmx4
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.129 — TBP-like
Superfamily Superfamily superfamily	d.129.2 — Phosphoglucomutase, C-terminal domain
Family Family family	d.129.2.1 — Phosphoglucomutase, C-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id	2fkmX01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	120 — Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3

Domain ID domain_id	2fkmX02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	120 — Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3

Domain ID domain_id	2fkmX03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	120 — Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3

Domain ID domain_id	2fkmX04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	310 — TATA-Binding Protein
Homologous superfamily homologous superfamily	50 — Alpha-D-phosphohexomutase, C-terminal domain

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Unit-cell length a length_a	70.222 Å
Unit-cell length b length_b	70.356 Å
Unit-cell length c length_c	84.392 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	1.900 Å
Low-resolution limit resolution_low	42.830 Å
R factor r_factor	0.2050
R_work r_work	0.2030
R_free r_free	0.2510

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

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

Phosphomannomutase/phosphoglucomutase

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

2fkm__assembly_1__model_1

2fkm__assembly_1__model_1 | I(q)

2fkm__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 (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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

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

Phosphomannomutase/phosphoglucomutase

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

2fkm__assembly_1__model_1

2fkm__assembly_1__model_1 | I(q)

2fkm__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 (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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)