SAXSdb — 1gec

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

GLYCYL ENDOPEPTIDASE

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE INHIBITOR × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PAP4_CARPA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain E； PDBConstruct 1–216； UniProt 133–348

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	1gec
Deposition date deposition_date	1995-05-25
Structure title title	GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25
Keywords keywords	PROTEINASE, 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.

1gec__assembly_1__model_1

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

Download this curve (.dat)

1gec__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gec__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.40 Å
Rg (electron density)	16.24 Å
Total Rg	17.27 Å
Atom count	1672
Residues	219
Excluded volume	29436 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gec__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 (3)

Entity 1 Entity 1 polymer

Description description	GLYCYL ENDOPEPTIDASE
Molecular weight formula_weight	23344.2 kDa
EC 编号 ec_number	3.4.22.25
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E
Atom count atom_count	1789

LPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDLQSYGCNRGYQSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEGSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKSGGKGYILIKNSWGPGWGENGYIRIRRASGNSPGVCGVYRSSYYPIKN

Entity 2 Entity 2 polymer

Description description	BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE INHIBITOR
Molecular weight formula_weight	464.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

XLVGX

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	117

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1gece_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.1 — Papain-like

CATH v4.4 (1 domains)

Domain ID domain_id	1gecE00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily	10 — Cysteine proteinases

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Unit-cell length a length_a	55.780 Å
Unit-cell length b length_b	55.780 Å
Unit-cell length c length_c	64.430 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	3

Space group space_group	P 31
Space-group number int_tables_number	144
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1960
R_work r_work	0.1960
R_free r_free	0.2580

GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25

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

GLYCYL ENDOPEPTIDASE

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

1gec__assembly_1__model_1

1gec__assembly_1__model_1 | I(q)

1gec__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25

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

GLYCYL ENDOPEPTIDASE

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

1gec__assembly_1__model_1

1gec__assembly_1__model_1 | I(q)

1gec__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)