SAXSdb — 1ems

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

NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN

Caenorhabditis elegans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	ETHYL MERCURY ION × 10 SODIUM ION × 8 (4S)-2-METHYL-2,4-PENTANEDIOL × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NFT1_CAEEL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–440； UniProt 1–440 Author chain B； PDBConstruct 1–440； UniProt 1–440

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	1ems
Deposition date deposition_date	2000-03-17
Structure title title	CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN
Keywords keywords	;WORM, NITRILASE, FHIT, NUCLEOTIDE-BINDING PROTEIN, CANCER, DIADENOSINE POLYPHOSPHATE HYDROLASE, HISTIDINE TRIAD, TUMOR SUPPRESSOR, ROSETTA STONE, ANTITUMOR PROTEIN ;; ANTITUMOR 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.

1ems__assembly_1__model_1

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

Download this curve (.dat)

1ems__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ems__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	38.87 Å
Rg (electron density)	38.85 Å
Total Rg	38.90 Å
Atom count	13094
Residues	1644
Excluded volume	232780 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ems__assembly_1__model_1`	tetrameric （4）	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 (5)

Entity 1 Entity 1 polymer

Description description	NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN
Molecular weight formula_weight	50007.9 kDa
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	6708

MLSTVFRRTMATGRHFIAVCQMTSDNDLEKNFQAAKNMIERAGEKKCEMVFLPECFDFIGLNKNEQIDLAMATDCEYMEKYRELARKHNIWLSLGGLHHKDPSDAAHPWNTHLIIDSDGVTRAEYNKLHLFDLEIPGKVRLMESEFSKAGTEMIPPVDTPIGRLGLSICYDVRFPELSLWNRKRGAQLLSFPSAFTLNTGLAHWETLLRARAIENQCYVVAAAQTGAHNPKRQSYGHSMVVDPWGAVVAQCSERVDMCFAEIDLSYVDTLREMQPVFSHRRSDLYTLHINEKSSETGGLKFARFNIPADHIFYSTPHSFVFVNLKPVTDGHVLVSPKRVVPRLTDLTDAETADLFIVAKKVQAMLEKHHNVTSTTICVQDGKDAGQTVPHVHIHILPRRAGDFGDNEIYQKLASHDKEPERKPRSNEQMAEEAVVYRNLM

Source Source

Source organism organism	Caenorhabditis elegans
NCBI taxonomy ID ncbi_taxonomy_id	6239
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ETHYL MERCURY ION
Molecular weight formula_weight	229.7 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 3 Entity 3 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	161

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1emsa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.13 — HIT-like
Superfamily Superfamily superfamily	d.13.1 — HIT-like
Family Family family	d.13.1.1 — HIT (HINT, histidine triad) family of protein kinase-interacting proteins

Domain ID domain_id	d1emsa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.1 — Nitrilase

Domain ID domain_id	d1emsb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.13 — HIT-like
Superfamily Superfamily superfamily	d.13.1 — HIT-like
Family Family family	d.13.1.1 — HIT (HINT, histidine triad) family of protein kinase-interacting proteins

Domain ID domain_id	d1emsb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.1 — Nitrilase

CATH v4.4 (4 domains)

Domain ID domain_id	1emsA01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

Domain ID domain_id	1emsA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	428 — HIT family, subunit A
Homologous superfamily homologous superfamily	10 — HIT-like

Domain ID domain_id	1emsB01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

Domain ID domain_id	1emsB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	428 — HIT family, subunit A
Homologous superfamily homologous superfamily	10 — HIT-like

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Unit-cell length a length_a	68.750 Å
Unit-cell length b length_b	100.440 Å
Unit-cell length c length_c	158.650 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 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1810
R_work r_work	0.1900
R_free r_free	0.2310

CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN

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

NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN

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

1ems__assembly_1__model_1

1ems__assembly_1__model_1 | I(q)

1ems__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (4)

CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN

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

NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN

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

1ems__assembly_1__model_1

1ems__assembly_1__model_1 | I(q)

1ems__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (4)