1hr8

Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide

Method: X-RAY DIFFRACTION

▼

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

MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT

Saccharomyces cerevisiae

UniProt P11914

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZINC ION × 1 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZINC ION × 1 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 12	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 4 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 4 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZINC ION × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MPPA_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–469； UniProt 14–482 Author chain C； PDBConstruct 1–469； UniProt 14–482 Author chain E； PDBConstruct 1–469； UniProt 14–482 Author chain G； PDBConstruct 1–469； UniProt 14–482

MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT

Saccharomyces cerevisiae

UniProt P10507

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZINC ION × 1 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZINC ION × 1 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 12	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 4 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 4 （P04037） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZINC ION × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MPPB_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–443； UniProt 21–462 Author chain D； PDBConstruct 2–443； UniProt 21–462 Author chain F； PDBConstruct 2–443； UniProt 21–462 Author chain H； PDBConstruct 2–443； UniProt 21–462

CYTOCHROME C OXIDASE POLYPEPTIDE IV

OrganismNot specified

UniProt P04037

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） ZINC ION × 1 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） ZINC ION × 1 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZINC ION × 1 water × 1	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 12	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 4 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 4 （P10507） 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZINC ION × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	COX4_YEAST
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain O； PDBConstruct 1–24； UniProt 2–25 Author chain P； PDBConstruct 1–24； UniProt 2–25 Author chain Q； PDBConstruct 1–24； UniProt 2–25 Author chain R； PDBConstruct 1–24； UniProt 2–25

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	1hr8
Deposition date deposition_date	2000-12-21
Structure title title	Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide
Keywords keywords	HxxEH zinc-binding motif, 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.

1hr8__assembly_1__model_1

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

Download this curve (.dat)

1hr8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hr8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.25 Å
Rg (electron density)	29.09 Å
Total Rg	29.92 Å
Atom count	7036
Residues	904
Excluded volume	125200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hr8__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1hr8__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1hr8__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1hr8__assembly_4__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1hr8__assembly_5__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 (6)

Entity 1 Entity 1 polymer

Description description	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT
Molecular weight formula_weight	52532.4 kDa
EC 编号 ec_number	3.4.24.64
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	27990

ARTDNFKLSSLANGLKVATSNTPGHFSALGLYIDAGSRFEGRNLKGCTHILDRLAFKSTEHVEGRAMAETLELLGGNYQCTSSRENLMYQASVFNQDVGKMLQLMSETVRFPKITEQELQEQKLSAEYEIDEVWMKPELVLPELLHTAAYSGETLGSPLICPRGLIPSISKYYLLDYRNKFYTPENTVAAFVGVPHEKALELTGKYLGDWQSTHPPITKKVAQYTGGESCIPPAPVFGNLPELFHIQIGFEGLPIDHPDIYALATLQTLLGGGGSFSAGGPGKGMYSRLYTHVLNQYYFVENCVAFNHSYSDSGIFGISLSCIPQAAPQAVEVIAQQMYNTFANKDLRLTEDEVSRAKNQLKSSLLMNLESKLVELEDMGRQVLMHGRKIPVNEMISKIEDLKPDDISRVAEMIFTGNVNNAGNGKGRATVVMQGDRGSFGDVENVLKAYGLGNSSSSKNDSPKKKGWFHHHHHH

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT
Molecular weight formula_weight	48894.0 kDa
EC 编号 ec_number	3.4.24.64
Mutation mutation	E73Q
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H

ASQIPGTRTSKLPNGLTIATEYIPNTSSATVGIFVDAGSRAENVKNNGTAHFLQHLAFKGTQNRPQQGIELEIENIGSHLNAYTSRENTVYYAKSLQEDIPKAVDILSDILTKSVLDNSAIERERDVIIRESEEVDKMYDEVVFDHLHEITYKDQPLGRTILGPIKNIKSITRTDLKDYITKNYKGDRMVLAGAGAVDHEKLVQYAQKYFGHVPKSESPVPLGSPRGPLPVFCRGERFIKENTLPTTHIAIALEGVSWSAPDYFVALATQAIVGNWDRAIGTGTNSPSPLAVAASQNGSLANSYMSFSTSYADSGLWGMYIVTDSNEHNVRLIVNEILKEWKRIKSGKISDAEVNRAKAQLKAALLLSLDGSTAIVEDIGRQVVTTGKRLSPEEVFEQVDKITKDDIIMWANYRLQNKPVSMVALGNTSTVPNVSYIEEKLNQ

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 polymer

Description description	CYTOCHROME C OXIDASE POLYPEPTIDE IV
Molecular weight formula_weight	2862.4 kDa
EC 编号 ec_number	1.9.3.1
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	O,P,Q,R

LSLRQSIRFFKPATRTLCSSRYLL

Entity 4 Entity 4 non-polymer

Description description	4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
Molecular weight formula_weight	238.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	4

▼

6. Fold Classification (SCOP + CATH) 34 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d1hr8a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8c1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8c2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8d1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8d2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8d3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1hr8e1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8e2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8f1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8f2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8f3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1hr8g1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8g2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8h1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d1hr8h2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

CATH v4.4 (16 domains)

Domain ID domain_id	1hr8A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8C01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8D01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8D02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8E01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8E02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8F01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8F02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8G01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8G02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8H01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	1hr8H02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

▶

Unit-cell length a length_a	134.260 Å
Unit-cell length b length_b	178.120 Å
Unit-cell length c length_c	202.210 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	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	48.630 Å
R factor r_factor	0.2290
R_work r_work	0.2290
R_free r_free	0.2640

Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide

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

MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

CYTOCHROME C OXIDASE POLYPEPTIDE IV

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

1hr8__assembly_1__model_1

1hr8__assembly_1__model_1 | I(q)

1hr8__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 (6)

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

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 34 domains

SCOP 2.08 (18 domains)

CATH v4.4 (16 domains)

7. Citations (1)

Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide

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

MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CYTOCHROME C OXIDASE POLYPEPTIDE IV

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

1hr8__assembly_1__model_1

1hr8__assembly_1__model_1 | I(q)

1hr8__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 (6)

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

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 34 domains

SCOP 2.08 (18 domains)

CATH v4.4 (16 domains)

7. Citations (1)