1cg2

CARBOXYPEPTIDASE G2

Method: X-RAY DIFFRACTION D_max: 135.1 Å Quality: GOOD

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

CARBOXYPEPTIDASE G2

Pseudomonas sp.

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 23–415 Chain B； UniProt 23–415 Chain C； UniProt 23–415 Chain D； UniProt 23–415	Not recorded	ZN ZINC ION × 13	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；HANGING DROPS WERE FORMED BY MIXING 4 MICROLITERS OF PROTEIN SOLUTION AT 16-20 MG/ML WITH 4 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 10-12% PEG 4000, 0.2M TRIS (PH 7.2), 0.2M ZINC ACETATE 10% GLYCEROL. CRYSTALS GREW AT 18-20 DEGREES WITHIN A FEW DAYS., vapor diffusion - hanging drop, temperature 291K	Resolution 2.50 Å R-free 0.224

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1CG2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–415（392 aa） Chain B 24–415（392 aa）	Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4	Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 24–415（392 aa） Chain D 24–415（392 aa）	Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 14 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4	Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 24–415（392 aa） Chain F 24–415（392 aa）	Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 17	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4	Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 24–415（392 aa） Chain H 24–415（392 aa）	Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 13	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4	Resolution 3.11 Å R-free 0.309
7M6U Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2 Deposited 2021-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 89–415（327 aa） Chain A 25–88（64 aa） Chain C 89–415（327 aa） Chain C 25–88（64 aa）	Mutation：K177A Mutation：K177A Mutation：K177A Mutation：K177A	ZN ZINC ION × 11 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Protein was prepared to a concentration of 19 mg/mL in 50 mM Tris 100 mM NaCl pH 7.4 0.2 mM ZnSO4. Reservoirs containing 750 uL of 20 mM Tris pH 8.0, 10% glycerol, and 10% PEG 3350 were prepared in 24 well hanging drop vapor diffusion plates. Equal volumes of protein solution and reservoir solution were mixed on a cover slip and suspended over the reservoir	Resolution 2.59 Å R-free 0.279
7M6U Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2 Deposited 2021-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 89–415（327 aa） Chain B 25–88（64 aa） Chain D 89–415（327 aa） Chain D 25–88（64 aa）	Mutation：K177A Mutation：K177A Mutation：K177A Mutation：K177A	ZN ZINC ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Protein was prepared to a concentration of 19 mg/mL in 50 mM Tris 100 mM NaCl pH 7.4 0.2 mM ZnSO4. Reservoirs containing 750 uL of 20 mM Tris pH 8.0, 10% glycerol, and 10% PEG 3350 were prepared in 24 well hanging drop vapor diffusion plates. Equal volumes of protein solution and reservoir solution were mixed on a cover slip and suspended over the reservoir	Resolution 2.59 Å R-free 0.279

2 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CBPG_PSES6
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–393； UniProt 23–415 Author chain B； PDBConstruct 1–393； UniProt 23–415 Author chain C； PDBConstruct 1–393； UniProt 23–415 Author chain D； PDBConstruct 1–393； UniProt 23–415

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cg2
Deposition date deposition_date	1996-12-20
Structure title title	CARBOXYPEPTIDASE G2
Keywords keywords	METALLOCARBOXYPEPTIDASE, HYDROLASE; METALLOCARBOXYPEPTIDASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	40.67 Å
Radius of gyration Rg (electron density) rg_electron	40.93 Å
Forward intensity I(0) i0	380739000.00
Molecular weight molecular_weight	158500.0 kDa
Excluded volume excluded_volume	197850 Å³
Envelope volume envelope_volume	261990 Å³
Hydration-shell volume shell_volume	55599 Å³
Envelope diameter envelope_diameter	135.3 Å
Shell Rg shell_rg	44.74 Å
Envelope Rg envelope_rg	39.62 Å
Shape Rg shape_rg	40.96 Å
Total Rg total_rg	41.02 Å
Total atoms total_atoms	11135
Residues n_residues	1556
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	135.1 Å
Rg (real space) rg_real	40.75 Å
Rg uncertainty (real space) rg_real_error	1.17 Å
I(0) (real space) i0_real	3.8070e+08
I(0) uncertainty (real space) i0_real_error	6.3960e+06
Rg (reciprocal space) rg_reciprocal	40.67 Å
I(0) (reciprocal space) i0_reciprocal	380700000.0000
Solution quality estimate total_estimate	0.8739
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	45.0 Å
Skewness Skewness skewness	0.372
Kurtosis Kurtosis kurtosis	-0.468
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	39130000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.751

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	CARBOXYPEPTIDASE G2
Molecular weight formula_weight	41748.4 kDa
EC 编号 ec_number	3.4.17.11
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	11466

ALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK

来源 Source

来源生物 organism	Pseudomonas sp.
NCBI Class编号 ncbi_taxonomy_id	312
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	13

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	331

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1cg2a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.4 — Bacterial dinuclear zinc exopeptidases

Domain ID domain_id	d1cg2a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.19 — Bacterial exopeptidase dimerisation domain
Family Family family	d.58.19.1 — Bacterial exopeptidase dimerisation domain

Domain ID domain_id	d1cg2b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.4 — Bacterial dinuclear zinc exopeptidases

Domain ID domain_id	d1cg2b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.19 — Bacterial exopeptidase dimerisation domain
Family Family family	d.58.19.1 — Bacterial exopeptidase dimerisation domain

Domain ID domain_id	d1cg2c1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.4 — Bacterial dinuclear zinc exopeptidases

Domain ID domain_id	d1cg2c2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.19 — Bacterial exopeptidase dimerisation domain
Family Family family	d.58.19.1 — Bacterial exopeptidase dimerisation domain

Domain ID domain_id	d1cg2d1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.4 — Bacterial dinuclear zinc exopeptidases

Domain ID domain_id	d1cg2d2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.19 — Bacterial exopeptidase dimerisation domain
Family Family family	d.58.19.1 — Bacterial exopeptidase dimerisation domain

CATH v4.4 (8 domains)

Domain ID domain_id	1cg2A01
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	1cg2A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	360 —

Domain ID domain_id	1cg2B01
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	1cg2B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	360 —

Domain ID domain_id	1cg2C01
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	1cg2C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	360 —

Domain ID domain_id	1cg2D01
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	1cg2D02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	360 —

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8. Citations (2)

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Unit-cell length a length_a	81.260 Å
Unit-cell length b length_b	105.280 Å
Unit-cell length c length_c	122.190 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	109.54 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1960
R_work r_work	0.1960
R_free r_free	0.2240

fit	/app/data/saxs_computation/cg/1cg2/1cg2.fit
pddf	/app/data/pr_computation/cg/1cg2/1cg2.pr.out
profile	/app/data/saxs_computation/cg/1cg2/1cg2.dat

CARBOXYPEPTIDASE G2

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

CARBOXYPEPTIDASE G2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)