1V26

Crystal structure of tt0168 from Thermus thermophilus HB8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001676	biological_process	long-chain fatty acid metabolic process
A	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
A	0005524	molecular_function	ATP binding
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001676	biological_process	long-chain fatty acid metabolic process
B	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
B	0005524	molecular_function	ATP binding
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 3001

Chain	Residue
A	THR184
A	GLU328
A	AMP1002
A	HOH3127

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 3002

Chain	Residue
B	THR184
B	GLU328
B	AMP2002

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MYR A 1001

Chain	Residue
A	VAL299
A	GLY302
A	GLY323
A	GLY325
A	VAL332
A	LYS439
A	AMP1002
A	THR214
A	TRP234

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP A 1002

Chain	Residue
A	GLY302
A	SER303
A	ALA304
A	GLN322
A	GLY323
A	TYR324
A	GLY325
A	LEU326
A	THR327
A	ASP418
A	ARG433
A	LYS435
A	LYS439
A	TRP444
A	MYR1001
A	MG3001
A	HOH3096
A	HOH3170
A	HOH3174

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MYR B 2001

Chain	Residue
B	THR214
B	TRP234
B	CYS235
B	VAL299
B	GLY302
B	GLY323
B	GLY325
B	VAL332
B	LYS439
B	AMP2002

---

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP B 2002

Chain	Residue
B	GLY302
B	SER303
B	ALA304
B	GLN322
B	GLY323
B	TYR324
B	GLY325
B	LEU326
B	THR327
B	ASP418
B	ARG433
B	LYS435
B	LYS439
B	TRP444
B	MYR2001
B	MG3002
B	HOH3055
B	HOH3063
B	HOH3166

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Functional Information from PROSITE/UniProt

site_id	PS00455
Number of Residues	12
Details	AMP_BINDING Putative AMP-binding domain signature. MAYTTGTTGlPK

Chain	Residue	Details
A	MET181-LYS192

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15145952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1V25","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15145952","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1V25","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15145952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1V26","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 198

Chain	Residue	Details
A	THR184	metal ligand
A	GLU328	metal ligand
A	LYS439	electrostatic stabiliser, hydrogen bond donor
A	TRP444	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 198

Chain	Residue	Details
B	THR184	metal ligand
B	GLU328	metal ligand
B	LYS439	electrostatic stabiliser, hydrogen bond donor
B	TRP444	electrostatic stabiliser, hydrogen bond donor

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