2abz

Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A

Method: X-RAY DIFFRACTION

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

Carboxypeptidase A1

Bos taurus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	Metallocarboxypeptidase inhibitor × 4 （P81511） ZINC ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CBPA1_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–309； UniProt 111–419 Author chain B； PDBConstruct 1–309； UniProt 111–419

Metallocarboxypeptidase inhibitor

Hirudo medicinalis

UniProt P81511

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	Carboxypeptidase A1 × 2 （P00730） ZINC ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MCPI_HIRME
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 2–67； UniProt 16–81 Author chain D； PDBConstruct 2–67； UniProt 16–81 Author chain E； PDBConstruct 2–67； UniProt 16–81 Author chain F； PDBConstruct 2–67； UniProt 16–81

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	2abz
Deposition date deposition_date	2005-07-18
Structure title title	Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A
Keywords keywords	inhibitor-metallocarboxypeptidase complex, LCI mutant, oxidative folding intermediate analog, 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.

2abz__assembly_1__model_1

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

Download this curve (.dat)

2abz__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2abz__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.69 Å
Rg (electron density)	29.80 Å
Total Rg	30.49 Å
Atom count	6504
Residues	826
Excluded volume	115130 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2abz__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 (3)

Entity 1 Entity 1 polymer

Description description	Carboxypeptidase A1
Molecular weight formula_weight	34721.8 kDa
EC 编号 ec_number	3.4.17.1
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	6504

ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTVNNLY

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	Pichia pastoris

Entity 2 Entity 2 polymer

Description description	Metallocarboxypeptidase inhibitor
Molecular weight formula_weight	7333.1 kDa
Mutation mutation	C19A/C43A
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

GSHTPDESFLCYQPDQVCAFICRGAAPLPSEGECNPHPTAPWAREGAVEWVPYSTGQCRTTCIPYVE

Source Source

Source organism organism	Hirudo medicinalis
Common name common_name	medicinal leech
NCBI taxonomy ID ncbi_taxonomy_id	6421
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2abza_
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.56.5.1 — Pancreatic carboxypeptidases

Domain ID domain_id	d2abzb_
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.56.5.1 — Pancreatic carboxypeptidases

Domain ID domain_id	d2abzc1
Class class	g — Small proteins
Fold Fold fold	g.30 — Carboxypeptidase inhibitor
Superfamily Superfamily superfamily	g.30.1 — Carboxypeptidase inhibitor
Family Family family	g.30.1.1 — Carboxypeptidase inhibitor

Domain ID domain_id	d2abzd_
Class class	g — Small proteins
Fold Fold fold	g.30 — Carboxypeptidase inhibitor
Superfamily Superfamily superfamily	g.30.1 — Carboxypeptidase inhibitor
Family Family family	g.30.1.1 — Carboxypeptidase inhibitor

Domain ID domain_id	d2abze_
Class class	g — Small proteins
Fold Fold fold	g.30 — Carboxypeptidase inhibitor
Superfamily Superfamily superfamily	g.30.1 — Carboxypeptidase inhibitor
Family Family family	g.30.1.1 — Carboxypeptidase inhibitor

Domain ID domain_id	d2abzf_
Class class	g — Small proteins
Fold Fold fold	g.30 — Carboxypeptidase inhibitor
Superfamily Superfamily superfamily	g.30.1 — Carboxypeptidase inhibitor
Family Family family	g.30.1.1 — Carboxypeptidase inhibitor

CATH v4.4 (6 domains)

Domain ID domain_id	2abzA00
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	2abzB00
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	2abzC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1040 — Carboxypeptidase Inhibitor; Chain A
Homologous superfamily homologous superfamily	10 — Carboxypeptidase inhibitor

Domain ID domain_id	2abzD00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1040 — Carboxypeptidase Inhibitor; Chain A
Homologous superfamily homologous superfamily	10 — Carboxypeptidase inhibitor

Domain ID domain_id	2abzE00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1040 — Carboxypeptidase Inhibitor; Chain A
Homologous superfamily homologous superfamily	10 — Carboxypeptidase inhibitor

Domain ID domain_id	2abzF00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1040 — Carboxypeptidase Inhibitor; Chain A
Homologous superfamily homologous superfamily	10 — Carboxypeptidase inhibitor

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Unit-cell length a length_a	124.930 Å
Unit-cell length b length_b	124.930 Å
Unit-cell length c length_c	154.980 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	32

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.160 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1900
R_work r_work	0.1890
R_free r_free	0.2340

Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A

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

Carboxypeptidase A1

State in the Current Structure

Other States of the Same Protein in the Database

Metallocarboxypeptidase inhibitor

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

2abz__assembly_1__model_1

2abz__assembly_1__model_1 | I(q)

2abz__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (3)

Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A

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

Carboxypeptidase A1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Metallocarboxypeptidase inhibitor

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

2abz__assembly_1__model_1

2abz__assembly_1__model_1 | I(q)

2abz__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (3)