1NKT

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006605	biological_process	protein targeting
A	0006886	biological_process	intracellular protein transport
A	0008564	molecular_function	protein-exporting ATPase activity
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0017038	biological_process	protein import
A	0031522	cellular_component	cell envelope Sec protein transport complex
A	0043952	biological_process	protein transport by the Sec complex
A	0065002	biological_process	intracellular protein transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006605	biological_process	protein targeting
B	0006886	biological_process	intracellular protein transport
B	0008564	molecular_function	protein-exporting ATPase activity
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0015031	biological_process	protein transport
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0017038	biological_process	protein import
B	0031522	cellular_component	cell envelope Sec protein transport complex
B	0043952	biological_process	protein transport by the Sec complex
B	0065002	biological_process	intracellular protein transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 951

Chain	Residue
A	LYS107
A	ADP900
A	HOH1294

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 952

Chain	Residue
B	ADP901
B	HOH1284

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site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP A 900

Chain	Residue
A	GLY104
A	GLU105
A	GLY106
A	LYS107
A	THR108
A	LEU109
A	TRP141
A	ASP493
A	ASN499
A	ASP501
A	ARG573
A	MG951
A	HOH1215
A	HOH1294
A	HOH1370
A	GLN80
A	ARG81
A	PHE83
A	GLN86

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site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP B 901

Chain	Residue
B	GLN80
B	ARG81
B	PHE83
B	GLN86
B	GLY104
B	GLU105
B	GLY106
B	LYS107
B	THR108
B	TRP141
B	ASP493
B	ASN499
B	ASP501
B	ARG573
B	MG952
B	HOH1217
B	HOH1384

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Functional Information from PROSITE/UniProt

site_id	PS01312
Number of Residues	16
Details	SECA SecA family signature. VtVATNMAGRGtDIvL

Chain	Residue	Details
A	VAL481-LEU496

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01382","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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