Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MR1

Crystal structure of methionine aminopeptidase from Rickettsia prowazekii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0004239	molecular_function	initiator methionyl aminopeptidase activity
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0004239	molecular_function	initiator methionyl aminopeptidase activity
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008235	molecular_function	metalloexopeptidase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity
C	0004177	molecular_function	aminopeptidase activity
C	0004239	molecular_function	initiator methionyl aminopeptidase activity
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008235	molecular_function	metalloexopeptidase activity
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
D	0004177	molecular_function	aminopeptidase activity
D	0004239	molecular_function	initiator methionyl aminopeptidase activity
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008235	molecular_function	metalloexopeptidase activity
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 249

Chain	Residue
A	ASP105
A	HIS168
A	GLU201
A	GLU233
A	MN250
A	PO4252

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 250

Chain	Residue
A	MN249
A	PO4252
A	HOH728
A	ASP94
A	ASP105
A	GLU233

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 251

Chain	Residue
A	ASN72
A	VAL74
A	SER229
A	HOH726

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PO4 A 252

Chain	Residue
A	HIS77
A	ASP94
A	ASP105
A	HIS168
A	HIS175
A	GLU201
A	GLU233
A	MN249
A	MN250
A	HOH728
A	HOH742
A	HOH744
A	HOH760

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 249

Chain	Residue
B	ASP105
B	HIS168
B	GLU201
B	GLU233
B	MN250
B	PO4252

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 250

Chain	Residue
B	ASP94
B	ASP105
B	GLU233
B	MN249
B	PO4252
B	HOH786

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 251

Chain	Residue
B	ASN72
B	VAL74
B	SER229
B	HOH309
B	HOH450

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PO4 B 252

Chain	Residue
B	HIS77
B	ASP94
B	ASP105
B	HIS168
B	HIS175
B	GLU201
B	GLU233
B	MN249
B	MN250
B	HOH785
B	HOH786
B	HOH787
B	HOH788
B	HOH799

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 249

Chain	Residue
C	ASP105
C	HIS168
C	GLU201
C	GLU233
C	MN250
C	PO4252

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 250

Chain	Residue
C	ASP94
C	ASP105
C	GLU233
C	MN249
C	PO4252
C	HOH712

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 251

Chain	Residue
C	ASN72
C	VAL74
C	SER229
C	HOH266
C	HOH277

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 252

Chain	Residue
C	HIS77
C	ASP94
C	ASP105
C	HIS168
C	HIS175
C	GLU201
C	GLU233
C	MN249
C	MN250
C	HOH626
C	HOH712

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 249

Chain	Residue
D	ASP105
D	HIS168
D	GLU201
D	GLU233
D	MN250
D	PO4252

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 250

Chain	Residue
D	HOH929
D	ASP94
D	ASP105
D	GLU233
D	MN249
D	PO4252

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 251

Chain	Residue
D	ASN72
D	VAL74
D	SER229
D	HOH280

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 D 252

Chain	Residue
D	HIS77
D	ASP94
D	ASP105
D	HIS168
D	PHE174
D	HIS175
D	GLU201
D	GLU233
D	MN249
D	MN250
D	HOH929

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 253

Chain	Residue
D	TYR60
D	PHE174
D	HIS175

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 254

Chain	Residue
D	LYS3
D	HIS5
D	ARG172

Functional Information from PROSITE/UniProt

site_id	PS00680
Number of Residues	19
Details	MAP_1 Methionine aminopeptidase subfamily 1 signature. YtGHGIGrvfHdkpsIl.NY

Chain	Residue	Details
A	TYR165-TYR183

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of methionine aminopeptidase from Rickettsia prowazekii.","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"],"authors":["Edwards T.E.","Abendroth J.","Sankaran B."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine.","authoringGroup":["Seattle Structural Genomics Center for Infectious Disease (SSGCID)"],"authors":["Edwards T.E.","Abendroth J.","Arakaki T.","Sankaran B."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine.","authoringGroup":["Seattle Structural Genomics Center for Infectious Disease (SSGCID)"],"authors":["Edwards T.E.","Abendroth J.","Arakaki T.","Sankaran B."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine.","authoringGroup":["Seattle Structural Genomics Center for Infectious Disease (SSGCID)"],"authors":["Edwards T.E.","Abendroth J.","Arakaki T.","Sankaran B."]}}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)