SAXSdb — 2adv

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

Glutaryl 7- Aminocephalosporanic Acid Acylase

Pseudomonas sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Glutaryl 7- Aminocephalosporanic Acid Acylase × 1 Glutaryl 7- Aminocephalosporanic Acid Acylase × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	G7AC_PSEU7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–166； UniProt 30–195

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	2adv
Deposition date deposition_date	2005-07-21
Structure title title	Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism
Keywords keywords	autoproteolysis, precursor activation, intermediate structure, cephalosporin acylase, HYDROLASE; HYDROLASE
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.

2adv__assembly_1__model_1

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

Download this curve (.dat)

2adv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2adv__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.88 Å
Rg (electron density)	25.81 Å
Total Rg	26.66 Å
Atom count	5372
Residues	683
Excluded volume	94236 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2adv__assembly_1__model_1`	trimeric （3）	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	Glutaryl 7- Aminocephalosporanic Acid Acylase
Molecular weight formula_weight	18205.9 kDa
EC 编号 ec_number	3.5.1.11
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	5746

EPTSTPQAPIAAYKPRSNEILWDGYGVPHIYGVDAPSAFYGYGWAQARSHGDNILRLYGEARGKGAEYWGPDYEQTTVWLLTNGVPERAQQWYAQQSPDFRANLDAFAAGINAYAQQNPDDISPDVRQVLPVSGADVVAHAHRLMNFLYVASPGRTLGEGDPPDLA

Source Source

Source organism organism	Pseudomonas sp.
NCBI taxonomy ID ncbi_taxonomy_id	405038
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Glutaryl 7- Aminocephalosporanic Acid Acylase
Molecular weight formula_weight	2951.3 kDa
EC 编号 ec_number	3.5.1.11
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SNSWAVAPGKTANGNALLLQNPHLSWTT

Source Source

Source organism organism	Pseudomonas sp.
NCBI taxonomy ID ncbi_taxonomy_id	405038
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Glutaryl 7- Aminocephalosporanic Acid Acylase
Molecular weight formula_weight	56185.6 kDa
EC 编号 ec_number	3.5.1.11
Mutation mutation	Y33L
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

DYFTLYEAHLVTPDFEIYGATQIGLPVIRFAFNQRMGITNTVNGMVGATNYRLTLQDGGYLYDGQVRPFERRQASYRLRQADGTTVDKPLEIRSSVHGPVFERADGTAVAVRVAGLDRPGMLEQYFDMITADSFDDYEAALARMQVPTFNIVYADREGTINYSFNGVAPKRAEGDIAFWQGLVPGDSSRYLWTETHPLDDLPRVTNPPGGFVQNSNDPPWTPTWPVTYTPKDFPSYLAPQTPHSLRAQQSVRLMSENDDLTLERFMALQLSHRAVMADRTLPDLIPAALIDPDPEVQAAARLLAAWDREFTSDSRAALLFEEWARLFAGQNFAGQAGFATPWSLDKPVSTPYGVRDPKAAVDQLRTAIANTKRKYGAIDRPFGDASRMILNDVNVPGAAGYGNLGSFRVFTWSDPDENGVRTPVHGETWVAMIEFSTPVRAYGLMSYGNSRQPGTTHYSDQIERVSRADFRELLLRREQVEAAVQERTPFNFKPHHHHHH

Source Source

Source organism organism	Pseudomonas sp.
NCBI taxonomy ID ncbi_taxonomy_id	405038
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	374

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	2advA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	439 — Penicillin Amidohydrolase; domain 1
Homologous superfamily homologous superfamily	10 — Penicillin Amidohydrolase, domain 1

Domain ID domain_id	2advC01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	2advC02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	120 — Penicillin G acylase, beta-roll domain
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain, beta-sheet knob region

Domain ID domain_id	2advC03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1400 — Penicillin amidase (Acylase) alpha subunit, N-terminal domain
Homologous superfamily homologous superfamily	10 — Aminohydrolase, alpha-helical knob region

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Unit-cell length a length_a	73.775 Å
Unit-cell length b length_b	73.775 Å
Unit-cell length c length_c	384.646 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 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.244 Å
Low-resolution limit resolution_low	48.220 Å
R factor r_factor	0.1848
R_work r_work	0.1834
R_free r_free	0.2104

Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

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

Glutaryl 7- Aminocephalosporanic Acid Acylase

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

2adv__assembly_1__model_1

2adv__assembly_1__model_1 | I(q)

2adv__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

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

Glutaryl 7- Aminocephalosporanic Acid Acylase

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

2adv__assembly_1__model_1

2adv__assembly_1__model_1 | I(q)

2adv__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)