2QGQ

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0006400	biological_process	tRNA modification
A	0016740	molecular_function	transferase activity
A	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0006400	biological_process	tRNA modification
B	0016740	molecular_function	transferase activity
B	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0006400	biological_process	tRNA modification
C	0016740	molecular_function	transferase activity
C	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0006400	biological_process	tRNA modification
D	0016740	molecular_function	transferase activity
D	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0006400	biological_process	tRNA modification
E	0016740	molecular_function	transferase activity
E	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0006400	biological_process	tRNA modification
F	0016740	molecular_function	transferase activity
F	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0003824	molecular_function	catalytic activity
G	0005737	cellular_component	cytoplasm
G	0006400	biological_process	tRNA modification
G	0016740	molecular_function	transferase activity
G	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0003824	molecular_function	catalytic activity
H	0005737	cellular_component	cytoplasm
H	0006400	biological_process	tRNA modification
H	0016740	molecular_function	transferase activity
H	0018339	biological_process	peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CXS A 501

Chain	Residue
A	PHE385
A	ARG404
A	GLU419
A	TRP426
G	ARG404
G	LYS418
G	GLU419
G	ASP421

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CXS B 501

Chain	Residue
B	GLU419
B	HOH575
B	HOH714
C	PHE385
C	GLU419
C	TRP426
B	ARG404

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CXS D 504

Chain	Residue
D	ARG404
D	LYS418
D	GLU419
D	TRP426
D	HOH593
D	HOH649
E	PHE385
E	ARG404
E	GLU419
E	TRP426

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CXS F 501

Chain	Residue
F	ARG404
F	LYS418
F	GLU419
F	ASP421
F	TRP426
H	PHE385
H	ARG404
H	GLU419
H	TRP426

---

Functional Information from PROSITE/UniProt

site_id	PS01278
Number of Residues	21
Details	MTTASE_RADICAL Methylthiotransferase radical SAM domain signature. VkIsdGCdrgCTFCsIpsfkG

Chain	Residue	Details
A	VAL142-GLY162

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01865","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23542644","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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