1kfi

Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium

Method: X-RAY DIFFRACTION

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

phosphoglucomutase 1

Paramecium tetraurelia

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	ZINC ION × 2 SULFATE ION × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PARF_PARTE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–572； UniProt 1–572 Author chain B； PDBConstruct 1–572； UniProt 1–572

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	1kfi
Deposition date deposition_date	2001-11-21
Structure title title	Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium
Keywords keywords	parafusin, phosphoprotein pp63, exocytosis, 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.

1kfi__assembly_1__model_1

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

Download this curve (.dat)

1kfi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1kfi__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.36 Å
Rg (electron density)	35.07 Å
Total Rg	35.41 Å
Atom count	9002
Residues	1140
Excluded volume	159470 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1kfi__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	phosphoglucomutase 1
Molecular weight formula_weight	63881.8 kDa
EC 编号 ec_number	5.4.2.2
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	9207

MQQVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLENFVQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLAYANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGIILTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTTKIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKVVDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGVAGPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYAHDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQFFVTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAAKNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHIREKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQFGRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNKADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSVGATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQFTGRNEPTVIT

Source Source

Source organism organism	Paramecium tetraurelia
NCBI taxonomy ID ncbi_taxonomy_id	5888
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	205

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1kfia1
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	d1kfia2
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	d1kfia3
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	d1kfia4
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

Domain ID domain_id	d1kfib1
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	d1kfib2
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	d1kfib3
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	d1kfib4
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 (8 domains)

Domain ID domain_id	1kfiA01
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	1kfiA02
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	1kfiA03
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	1kfiA04
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

Domain ID domain_id	1kfiB01
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	1kfiB02
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	1kfiB03
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	1kfiB04
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	67.346 Å
Unit-cell length b length_b	133.609 Å
Unit-cell length c length_c	150.545 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	2.400 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	—
R_work r_work	0.2270
R_free r_free	0.2860

Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium

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

phosphoglucomutase 1

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

1kfi__assembly_1__model_1

1kfi__assembly_1__model_1 | I(q)

1kfi__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium

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

phosphoglucomutase 1

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

1kfi__assembly_1__model_1

1kfi__assembly_1__model_1 | I(q)

1kfi__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)