1hr8

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

Method: X-RAY DIFFRACTION D_max: 169.9 Å Quality: GOOD

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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	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 14–482	Not recorded	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 14–482	Not recorded	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain E； UniProt 14–482	Not recorded	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain G； UniProt 14–482	Not recorded	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
5	Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 14–482 Chain C； UniProt 14–482 Chain E； UniProt 14–482 Chain G； UniProt 14–482	Not recorded	MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 4 （P10507） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 4 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264

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 1HR8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 14–482（469 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 14–482（469 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 14–482（469 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 14–482（469 aa）	Not recorded	ZN ZINC ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 14–482（469 aa）	Not recorded	ZN ZINC ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256

3 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 21–462	Mutation：E73Q	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 21–462	Mutation：E73Q	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain F； UniProt 21–462	Mutation：E73Q	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain H； UniProt 21–462	Mutation：E73Q	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 1 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
5	Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain B； UniProt 21–462 Chain D； UniProt 21–462 Chain F； UniProt 21–462 Chain H； UniProt 21–462	Mutation：E73Q	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 4 （P11914） CYTOCHROME C OXIDASE POLYPEPTIDE IV × 4 （P04037） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1HR8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 21–462（442 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 21–462（442 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 21–462（442 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR6 Yeast Mitochondrial Processing Peptidase Deposited 2000-12-21	Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 21–462（442 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.279
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR7 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Deposited 2000-12-21	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256
1HR9 Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide Deposited 2000-12-21	Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 21–462（442 aa）	Mutation：E73Q	ZN ZINC ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.01 Å R-free 0.256

3 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain O； UniProt 2–25	Fragment：RESIDUES 2-25	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain P； UniProt 2–25	Fragment：RESIDUES 2-25	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain Q； UniProt 2–25	Fragment：RESIDUES 2-25	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain R； UniProt 2–25	Fragment：RESIDUES 2-25	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 1 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 1 （P10507） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264
5	Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain O； UniProt 2–25 Chain P； UniProt 2–25 Chain Q； UniProt 2–25 Chain R； UniProt 2–25	Fragment：RESIDUES 2-25	MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT × 4 （P11914） MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT × 4 （P10507） EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.70 Å R-free 0.264

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1HR8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2ODX Solution structure of Zn(II)Cox4 Deposited 2006-12-27	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 79–155（77 aa） Fragment：Cox4 subunit	Not recorded	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 50 mM phosphate, 200 mM NaCl；Pressure 1 NMR sample composition 1 mM Zn(II)Cox4 U-15N, 50mM phosphate buffer NA, 200 mM NaCl, 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM Zn(II)Cox4 U-15N,13C, 50mM phosphate buffer NA, 200 mM NaCl, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
6HU9 III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae Deposited 2018-10-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric	Chain d 26–155（130 aa） Chain p 26–155（130 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec	Resolution 3.35 Å
6T0B The III2-IV(5B)2 respiratory supercomplex from S. cerevisiae Deposited 2019-10-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 46 PDB declaration: 46-meric	Chain d 26–155（130 aa） Chain q 26–155（130 aa）	Not recorded	CDL CARDIOLIPIN × 8 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 7 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s	Resolution 2.80 Å
6T15 The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae Deposited 2019-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain d 26–155（130 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 18 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 CDL CARDIOLIPIN × 7 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s	Resolution 3.29 Å
6YMX CIII2/CIV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2020-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric	Chain d 30–146（117 aa）	Not recorded	CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 5 ZN ZINC ION × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
6YMY Cytochrome c oxidase from Saccharomyces cerevisiae Deposited 2020-04-10	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain d 30–146（117 aa）	Not recorded	CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.41 Å
7Z10 Monomeric respiratory complex IV isolated from S. cerevisiae Deposited 2022-02-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain d 29–149（121 aa）	Not recorded	CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；3 microliters of sample applied to negatively glow discharged grig.	Resolution 3.87 Å
8DH6 Cryo-EM structure of Saccharomyces cerevisiae cytochrome c oxidase (Complex IV) extracted in lipid nanodiscs Deposited 2022-06-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain d 26–155（130 aa）	Not recorded	CA CALCIUM ION × 1 MG MAGNESIUM ION × 1 CU COPPER (II) ION × 2 HEA HEME-A × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 10 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
8E7S III2IV2 respiratory supercomplex from Saccharomyces cerevisiae with 4 bound UQ6 Deposited 2022-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric	Chain T 1–155（155 aa） Chain t 1–155（155 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 24 FES FE2/S2 (INORGANIC) CLUSTER × 2 CDL CARDIOLIPIN × 10 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEA HEME-A × 4 CU COPPER (II) ION × 2 CUA DINUCLEAR COPPER ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8EC0 III2IV respiratory supercomplex from Saccharomyces cerevisiae cardiolipin-lacking mutant Deposited 2022-08-31	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain T 1–155（155 aa）	Not recorded	PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 15 PGT (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 7 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9BPB Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae Deposited 2024-05-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 42 PDB declaration: 42-meric	Chain d 1–155（155 aa） Chain p 1–155（155 aa）	Not recorded	CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force.	Resolution 2.57 Å
9ETZ III2IV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2024-03-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric	Chain d 30–149（120 aa）	Not recorded	CDL CARDIOLIPIN × 11 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CA CALCIUM ION × 1 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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.

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	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

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

Radius of gyration Rg (Guinier) rg_guinier	55.66 Å
Radius of gyration Rg (electron density) rg_electron	55.24 Å
Forward intensity I(0) i0	2248200000.00
Molecular weight molecular_weight	397800.0 kDa
Excluded volume excluded_volume	498010 Å³
Envelope volume envelope_volume	723100 Å³
Hydration-shell volume shell_volume	107670 Å³
Envelope diameter envelope_diameter	172.9 Å
Shell Rg shell_rg	59.76 Å
Envelope Rg envelope_rg	53.56 Å
Shape Rg shape_rg	55.24 Å
Total Rg total_rg	55.36 Å
Total atoms total_atoms	27986
Residues n_residues	3598
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	169.9 Å
Rg (real space) rg_real	55.41 Å
Rg uncertainty (real space) rg_real_error	1.54 Å
I(0) (real space) i0_real	2.2480e+09
I(0) uncertainty (real space) i0_real_error	4.3880e+07
Rg (reciprocal space) rg_reciprocal	55.84 Å
I(0) (reciprocal space) i0_reciprocal	2250000000.0000
Solution quality estimate total_estimate	0.8325
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	85.0 Å
Skewness Skewness skewness	0.063
Kurtosis Kurtosis kurtosis	-0.658
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	326400000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. 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

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 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

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 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

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7. 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

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8. Citations (1)

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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

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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 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

7. Fold Classification (SCOP + CATH) 34 domains

SCOP 2.08 (18 domains)

CATH v4.4 (16 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/hr/1hr8/1hr8.fit
pddf	/app/data/pr_computation/hr/1hr8/1hr8.pr.out
profile	/app/data/saxs_computation/hr/1hr8/1hr8.dat