SAXSdb — 7g1p

▼

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

Fatty acid-binding protein, adipocyte

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	6-chloro-5-fluoro-1H-benzimidazole × 1 MYRISTIC ACID × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FABP4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–135； UniProt 1–132

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	7g1p
Deposition date deposition_date	2023-04-27
Structure title title	Crystal Structure of human FABP4 binding site mutated to that of FABP5 in complex with 6-chloro-5-fluoro-1H-benzimidazole
Keywords keywords	LIPID BINDING PROTEIN, FATTY ACID BINDING PROTEIN, CYTOPLASM, LIPID-BINDING, TRANSPORT, PROTEIN BINDING; LIPID BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

7g1p__assembly_1__model_1

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

Download this curve (.dat)

7g1p__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7g1p__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.19 Å
Rg (electron density)	13.84 Å
Total Rg	15.11 Å
Atom count	1039
Residues	130
Excluded volume	18712 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7g1p__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Fatty acid-binding protein, adipocyte
Molecular weight formula_weight	15012.2 kDa
Mutation mutation	V24L,V33M,A34G,M41C,S54T,F58L,H94Q,S125C
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1218

GSHMCDAFVGTWKLVSSENFDDYMKELGVGFATRKMGGMAKPNCIISVNGDVITIKTESTLKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVQVQKWDGKSTTIKRKREDDKLVVECVMKGVTCTRVYERA

Source Source

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

Entity 2 Entity 2 non-polymer

Description description	6-chloro-5-fluoro-1H-benzimidazole
Molecular weight formula_weight	170.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 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	146

▼

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	7g1pA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	20 — Calycin beta-barrel core domain

▶

Unit-cell length a length_a	32.158 Å
Unit-cell length b length_b	52.964 Å
Unit-cell length c length_c	72.240 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 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.280 Å
Low-resolution limit resolution_low	42.720 Å
R factor r_factor	0.1796
R_work r_work	0.1763
R_free r_free	0.2417

Crystal Structure of human FABP4 binding site mutated to that of FABP5 in complex with 6-chloro-5-fluoro-1H-benzimidazole

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

Fatty acid-binding protein, adipocyte

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

7g1p__assembly_1__model_1

7g1p__assembly_1__model_1 | I(q)

7g1p__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) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Crystal Structure of human FABP4 binding site mutated to that of FABP5 in complex with 6-chloro-5-fluoro-1H-benzimidazole

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

Fatty acid-binding protein, adipocyte

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

7g1p__assembly_1__model_1

7g1p__assembly_1__model_1 | I(q)

7g1p__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) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)