SAXSdb — 1fi8

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

NATURAL KILLER CELL PROTEASE 1

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	ECOTIN × 2 （P23827） ECOTIN × 2 （P23827） water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NKP1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–228； UniProt 21–248 Author chain B； PDBConstruct 1–228； UniProt 21–248

ECOTIN

Escherichia coli

UniProt P23827

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	NATURAL KILLER CELL PROTEASE 1 × 2 （P18291） water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ECOT_ECOLI
Isoform	—
PDB entities	2, 3
Chains and sequence ranges	Author chain C； PDBConstruct 6–84； UniProt 21–100 Author chain E； PDBConstruct 6–84； UniProt 21–100 Author chain D； PDBConstruct 1–58； UniProt 105–162 Author chain F； PDBConstruct 1–58； UniProt 105–162

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	1fi8
Deposition date deposition_date	2000-08-03
Structure title title	RAT GRANZYME B [N66Q] COMPLEXED TO ECOTIN [81-84 IEPD]
Keywords keywords	;complex (serine protease-inhibitor), protease substrate interactions, beta strand structure, chymotrypsin fold, granzyme B, ecotin, HYDROLASE-HYDROLASE INHIBITOR COMPLEX ;; HYDROLASE/HYDROLASE INHIBITOR
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.

1fi8__assembly_1__model_1

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

Download this curve (.dat)

1fi8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1fi8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	31.17 Å
Rg (electron density)	30.88 Å
Total Rg	31.55 Å
Atom count	5268
Residues	703
Excluded volume	93985 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1fi8__assembly_1__model_1`	hexameric （6）	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	NATURAL KILLER CELL PROTEASE 1
Molecular weight formula_weight	25225.4 kDa
EC 编号 ec_number	3.4.21.-
Mutation mutation	N66Q
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	5638

IIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKIQVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Pichia pastoris

Entity 2 Entity 2 polymer

Description description	ECOTIN
Molecular weight formula_weight	9528.7 kDa
Mutation mutation	V81I, S82E, T83P, M84D
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,E

AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLEGWGYDYYVFDKVSSPIEPD

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	ECOTIN
Molecular weight formula_weight	6645.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,F

MACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	370

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1fi8.1
Class class	b — All beta proteins
Fold Fold fold	b.16 — Ecotin, trypsin inhibitor
Superfamily Superfamily superfamily	b.16.1 — Ecotin, trypsin inhibitor
Family Family family	b.16.1.1 — Ecotin, trypsin inhibitor

Domain ID domain_id	d1fi8.2
Class class	b — All beta proteins
Fold Fold fold	b.16 — Ecotin, trypsin inhibitor
Superfamily Superfamily superfamily	b.16.1 — Ecotin, trypsin inhibitor
Family Family family	b.16.1.1 — Ecotin, trypsin inhibitor

Domain ID domain_id	d1fi8a_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

Domain ID domain_id	d1fi8b_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

CATH v4.4 (8 domains)

Domain ID domain_id	1fi8A01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1fi8A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1fi8B01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1fi8B02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1fi8C00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	550 — Ecotin

Domain ID domain_id	1fi8D00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	1230 — Ecotin, trypsin inhibitor
Homologous superfamily homologous superfamily	10 — Ecotin, trypsin inhibitor

Domain ID domain_id	1fi8E00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	550 — Ecotin

Domain ID domain_id	1fi8F00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	1230 — Ecotin, trypsin inhibitor
Homologous superfamily homologous superfamily	10 — Ecotin, trypsin inhibitor

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Unit-cell length a length_a	56.640 Å
Unit-cell length b length_b	154.600 Å
Unit-cell length c length_c	57.240 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	119.76 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	35.700 Å
R factor r_factor	0.2220
R_work r_work	0.2180
R_free r_free	0.2520

RAT GRANZYME B [N66Q] COMPLEXED TO ECOTIN [81-84 IEPD]

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

NATURAL KILLER CELL PROTEASE 1

State in the Current Structure

Other States of the Same Protein in the Database

ECOTIN

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

1fi8__assembly_1__model_1

1fi8__assembly_1__model_1 | I(q)

1fi8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)

RAT GRANZYME B [N66Q] COMPLEXED TO ECOTIN [81-84 IEPD]

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

NATURAL KILLER CELL PROTEASE 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

ECOTIN

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

1fi8__assembly_1__model_1

1fi8__assembly_1__model_1 | I(q)

1fi8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)