SAXSdb — 4njq

▼

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

Probable M18 family aminopeptidase 2

Pseudomonas aeruginosa

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 12	COBALT (II) ION × 24 CARBONATE ION × 12 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 9 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	APEB_PSEAE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–429； UniProt 1–429 Author chain B； PDBConstruct 1–429； UniProt 1–429 Author chain C； PDBConstruct 1–429； UniProt 1–429 Author chain D； PDBConstruct 1–429； UniProt 1–429

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	4njq
Deposition date deposition_date	2013-11-11
Structure title title	Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa
Keywords keywords	metallopeptidase, aspartyl aminopeptidase, cobalt complex, Tetrahedral shape dodecameric structure, Metal binding, HYDROLASE; HYDROLASE
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.

4njq__assembly_1__model_1

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

Download this curve (.dat)

4njq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4njq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	51.91 Å
Rg (electron density)	51.14 Å
Total Rg	51.47 Å
Atom count	38145
Residues	4899
Excluded volume	671570 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4njq__assembly_1__model_1`	dodecameric （12）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Probable M18 family aminopeptidase 2
Molecular weight formula_weight	46713.4 kDa
EC 编号 ec_number	3.4.11.-
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	12818

MRAELNQGLIDFLKASPTPFHATASLARRLEAAGYRRLDERDAWHTETGGRYYVTRNDSSLIAIRLGRRSPLESGFRLVGAHTDSPCLRVKPNPEIARNGFLQLGVEVYGGALFAPWFDRDLSLAGRVTFRANGKLESRLVDFRKAIAVIPNLAIHLNRAANEGWPINAQNELPPIIAQLAPGEAADFRLLLDEQLLREHGITADVVLDYELSFYDTQSAAVVGLNDEFIAGARLDNLLSCHAGLEALLNAEGDENCILVCTDHEEVGSCSHCGADGPFLEQVLRRLLPEGDAFSRAIQRSLLVSADNAHGVHPNYADRHDANHGPALNGGPVIKINSNQRYATNSETAGFFRHLCQDSEVPVQSFVTRSDMGCGSTIGPITASQVGVRTVDIGLPTFAMHSIRELAGSHDLAHLVKVLGAFYASSELP

Source Source

Source organism organism	Pseudomonas aeruginosa
NCBI taxonomy ID ncbi_taxonomy_id	208964
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	COBALT (II) ION
Molecular weight formula_weight	58.9 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 non-polymer

Description description	CARBONATE ION
Molecular weight formula_weight	60.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
Molecular weight formula_weight	207.3 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	103

▼

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	4njqA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	10 — Zn peptidases

Domain ID domain_id	4njqA02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	250 — Aminopeptidase i, Domain 2
Homologous superfamily homologous superfamily	10 — Aminopeptidase i, Domain 2

Domain ID domain_id	4njqB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	10 — Zn peptidases

Domain ID domain_id	4njqB02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	250 — Aminopeptidase i, Domain 2
Homologous superfamily homologous superfamily	10 — Aminopeptidase i, Domain 2

Domain ID domain_id	4njqC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	10 — Zn peptidases

Domain ID domain_id	4njqC02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	250 — Aminopeptidase i, Domain 2
Homologous superfamily homologous superfamily	10 — Aminopeptidase i, Domain 2

Domain ID domain_id	4njqD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	10 — Zn peptidases

Domain ID domain_id	4njqD02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	250 — Aminopeptidase i, Domain 2
Homologous superfamily homologous superfamily	10 — Aminopeptidase i, Domain 2

▶

Unit-cell length a length_a	133.205 Å
Unit-cell length b length_b	133.205 Å
Unit-cell length c length_c	322.316 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	36

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.702 Å
Low-resolution limit resolution_low	42.764 Å
R factor r_factor	0.1702
R_work r_work	0.1673
R_free r_free	0.2230

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

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

Probable M18 family aminopeptidase 2

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

4njq__assembly_1__model_1

4njq__assembly_1__model_1 | I(q)

4njq__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

CATH v4.4 (8 domains)

7. Citations (1)

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

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

Probable M18 family aminopeptidase 2

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

4njq__assembly_1__model_1

4njq__assembly_1__model_1 | I(q)

4njq__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

CATH v4.4 (8 domains)

7. Citations (1)