Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NYY

human m-AAA protease AFG3L2, substrate-bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0005524	molecular_function	ATP binding
A	0006508	biological_process	proteolysis
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0005524	molecular_function	ATP binding
B	0006508	biological_process	proteolysis
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004222	molecular_function	metalloendopeptidase activity
C	0005524	molecular_function	ATP binding
C	0006508	biological_process	proteolysis
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004222	molecular_function	metalloendopeptidase activity
D	0005524	molecular_function	ATP binding
D	0006508	biological_process	proteolysis
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004222	molecular_function	metalloendopeptidase activity
E	0005524	molecular_function	ATP binding
E	0006508	biological_process	proteolysis
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004222	molecular_function	metalloendopeptidase activity
F	0005524	molecular_function	ATP binding
F	0006508	biological_process	proteolysis
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ZN A 801

Chain	Residue
A	HIS574
A	HIS578
A	ASP649

site_id	AC2
Number of Residues	17
Details	binding site for residue ANP B 801

Chain	Residue
B	THR355
B	LEU356
B	GLN408
B	ASN454
B	ILE486
B	HIS490
B	GLY518
B	MG802
C	ASP439
C	ARG465
C	ARG468
B	ASP309
B	VAL310
B	GLY351
B	THR352
B	GLY353
B	LYS354

site_id	AC3
Number of Residues	3
Details	binding site for residue MG B 802

Chain	Residue
B	THR355
B	ASP407
B	ANP801

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 803

Chain	Residue
B	HIS574
B	HIS578
B	ASP649
H	ALA6

site_id	AC5
Number of Residues	2
Details	binding site for residue MG C 801

Chain	Residue
C	THR355
C	ANP803

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN C 802

Chain	Residue
C	HIS574
C	HIS578
C	ASP649
I	ALA5

site_id	AC7
Number of Residues	18
Details	binding site for residue ANP D 801

Chain	Residue
D	ASP309
D	ALA311
D	GLY351
D	THR352
D	GLY353
D	LYS354
D	THR355
D	LEU356
D	GLN408
D	ASN454
D	ILE486
D	HIS490
D	GLY518
D	ALA519
D	MG802
E	ASP439
E	ARG465
E	ARG468

site_id	AC8
Number of Residues	4
Details	binding site for residue MG D 802

Chain	Residue
D	THR355
D	ASP407
D	ANP801
E	ASP439

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN D 803

Chain	Residue
D	HIS574
D	HIS578
D	ASP649
J	ALA5

site_id	AD1
Number of Residues	12
Details	binding site for residue ADP E 801

Chain	Residue
E	ASP309
E	ALA311
E	GLY351
E	THR352
E	GLY353
E	LYS354
E	THR355
E	LEU356
E	ILE486
E	HIS490
E	GLY518
E	ALA519

site_id	AD2
Number of Residues	3
Details	binding site for residue ZN E 802

Chain	Residue
E	HIS574
E	HIS578
E	ASP649

site_id	AD3
Number of Residues	3
Details	binding site for residue ZN F 801

Chain	Residue
F	HIS574
F	HIS578
F	ASP649

site_id	AD4
Number of Residues	17
Details	binding site for Di-peptide ANP C 803 and GLY C 353

Chain	Residue
C	ASP309
C	ALA311
C	PRO350
C	GLY351
C	THR352
C	LYS354
C	THR355
C	LEU356
C	LEU357
C	GLN408
C	ILE486
C	HIS490
C	GLY518
C	ALA519
C	MG801
D	ARG465
D	ARG468

site_id	AD5
Number of Residues	39
Details	binding site for Di-peptide ANP C 803 and ARG D 468

Chain	Residue
C	GLY351
C	THR352
C	GLY353
C	LYS354
C	THR355
C	LEU356
C	GLN408
C	LEU435
C	MET438
C	ASP439
C	ALA462
C	LEU463
C	ARG465
C	PRO466
C	GLY467
C	PHE469
C	ILE486
C	HIS490
C	GLY518
C	ALA519
C	MG801
D	LEU435
D	MET438
D	ASP439
D	ALA462
D	LEU463
D	ARG465
D	PRO466
D	GLY467
D	PHE469
D	HIS574
D	HIS578
D	ASP649
J	ALA5
B	ANP801
C	ASP309
C	ALA311
C	LYS342
C	PRO350

Functional Information from PROSITE/UniProt

site_id	PS00674
Number of Residues	19
Details	AAA AAA-protein family signature. VvILaGTNrpdiLDpALl.R

Chain	Residue	Details
A	VAL447-ARG465

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3150
Details	TOPO_DOM: Mitochondrial matrix => ECO:0000305\|PubMed:31327635

Chain	Residue	Details
A	ARG272-ASN797
B	ARG272-ASN797
C	ARG272-ASN797
D	ARG272-ASN797
E	ARG272-ASN797
F	ARG272-ASN797

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000305\|PubMed:31327635

Chain	Residue	Details
A	GLN575
B	GLN575
C	GLN575
D	GLN575
E	GLN575
F	GLN575

site_id	SWS_FT_FI3
Number of Residues	48
Details	BINDING: BINDING => ECO:0000305\|PubMed:31327635, ECO:0007744\|PDB:6NYY

Chain	Residue	Details
A	VAL310
B	ALA311
B	THR352
B	GLY353
B	LYS354
B	THR355
B	LEU356
B	HIS490
C	VAL310
C	ALA311
C	THR352
A	ALA311
C	GLY353
C	LYS354
C	THR355
C	LEU356
C	HIS490
D	VAL310
D	ALA311
D	THR352
D	GLY353
D	LYS354
A	THR352
D	THR355
D	LEU356
D	HIS490
E	VAL310
E	ALA311
E	THR352
E	GLY353
E	LYS354
E	THR355
E	LEU356
A	GLY353
E	HIS490
F	VAL310
F	ALA311
F	THR352
F	GLY353
F	LYS354
F	THR355
F	LEU356
F	HIS490
A	LYS354
A	THR355
A	LEU356
A	HIS490
B	VAL310

site_id	SWS_FT_FI4
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:31327635, ECO:0007744\|PDB:6NYY

Chain	Residue	Details
A	HIS574
D	HIS574
D	HIS578
D	ASP649
E	HIS574
E	HIS578
E	ASP649
F	HIS574
F	HIS578
F	ASP649
A	HIS578
A	ASP649
B	HIS574
B	HIS578
B	ASP649
C	HIS574
C	HIS578
C	ASP649

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)