SAXSdb — 1nf1

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

PROTEIN (NEUROFIBROMIN)

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NF1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–333； UniProt 864–1196

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	1nf1
Deposition date deposition_date	1998-07-08
Structure title title	THE GAP RELATED DOMAIN OF NEUROFIBROMIN
Keywords keywords	;NEUROFIBROMIN, TYPE I NEUROFIBROMATOSIS, NF1, RAS, GAP, SIGNAL TRANSDUCTION, CANCER, GROWTH REGULATION, GTP HYDROLYSIS, PATIENT MUTATION, ARGININE FINGER, SIGNALING PROTEIN ;; SIGNALING PROTEIN
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.

1nf1__assembly_1__model_1

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

Download this curve (.dat)

1nf1__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1nf1__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.04 Å
Rg (electron density)	21.20 Å
Total Rg	22.04 Å
Atom count	1947
Residues	259
Excluded volume	35052 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1nf1__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 (1)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1nf1a_
Class class	a — All alpha proteins
Fold Fold fold	a.116 — GTPase activation domain, GAP
Superfamily Superfamily superfamily	a.116.1 — GTPase activation domain, GAP
Family Family family	a.116.1.2 — p120GAP domain-like

CATH v4.4 (2 domains)

Domain ID domain_id	1nf1A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily	10 — GTPase Activation - p120gap; domain 1

Domain ID domain_id	1nf1A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily	10 — GTPase Activation - p120gap; domain 1

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7. Citations (11)

Structural analysis of the GAP-related domain from neurofibromin and its implications.

EMBO J. (1998)

PMID: 9687500 · DOI: 10.1093/emboj/17.15.4313 PRIMARY

The Ras-Rasgap Complex: Structural Basis for Gtpase Activation and its Loss in Oncogenic Ras Mutants

Science (1997)

DOI: 10.1126/science.277.5324.333

Confirmation of the Arginine-Finger Hypothesis for the Gap-Stimulated GTP- Hydrolysis Reaction of Ras

Nat.Struct.Biol. (1997)

Structural Differences in the Minimal Catalytic Domains of the Gtpasse- Activating Proteins P120Gap and Neurofibromin

J.Biol.Chem. (1996)

DOI: 10.1074/jbc.271.27.16409

3-Dimensional Structure of the Gtpase Activating Domain of Human P120Gap and Implications for the Interaction with Ras

Nature (1996)

DOI: 10.1038/384591a0

Formation of a Transition-State Analog of the Ras Gtpase Reaction by Ras:Gdp, Tetrafluoroaluminate and Gtpase-Activating Proteins

Science (1996)

The Neurofibromatosis Type I Gene and its Protein Product

Neuron (1993)

;Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 A Resolution: Implications for the Mechanism of GTP Hydrolysis ;

Embo J. (1990)

The NF1 Locus Encodes a Protein Functionally Related to Mammalian Gap and Yeast Ira Proteins

Cell(Cambridge,Mass.) (1990)

DOI: 10.1016/0092-8674(90)90151-4

The Gap-Related Domain of the Neurofibromatosis Type I Gene Product Interacts with Ras P21

Cell(Cambridge,Mass.) (1990)

DOI: 10.1016/0092-8674(90)90150-D

;The Catalytic Domain of the Neurofibromatosis Type I Gene Product Stimulates Ras Gtpase and Complements Ira Mutants of S. Cerevisiae ;

Cell(Cambridge,Mass.) (1990)

DOI: 10.1016/0092-8674(90)90149-9

Unit-cell length a length_a	88.250 Å
Unit-cell length b length_b	58.300 Å
Unit-cell length c length_c	74.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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	30.000 Å
R factor r_factor	0.2660
R_work r_work	0.2660
R_free r_free	0.3690

Description description	PROTEIN (NEUROFIBROMIN)
Molecular weight formula_weight	37982.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1948

THE GAP RELATED DOMAIN OF NEUROFIBROMIN

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

PROTEIN (NEUROFIBROMIN)

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

1nf1__assembly_1__model_1

1nf1__assembly_1__model_1 | I(q)

1nf1__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (11)

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

THE GAP RELATED DOMAIN OF NEUROFIBROMIN

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

PROTEIN (NEUROFIBROMIN)

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

1nf1__assembly_1__model_1

1nf1__assembly_1__model_1 | I(q)

1nf1__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (11)