2PKF

Crystal structure of M tuberculosis Adenosine Kinase (apo)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004001	molecular_function	adenosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0005886	cellular_component	plasma membrane
A	0006166	biological_process	purine ribonucleoside salvage
A	0016301	molecular_function	kinase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0032567	molecular_function	dGTP binding
A	0044209	biological_process	AMP salvage
B	0000287	molecular_function	magnesium ion binding
B	0004001	molecular_function	adenosine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005886	cellular_component	plasma membrane
B	0006166	biological_process	purine ribonucleoside salvage
B	0016301	molecular_function	kinase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0032567	molecular_function	dGTP binding
B	0044209	biological_process	AMP salvage

Functional Information from PROSITE/UniProt

site_id	PS00583
Number of Residues	25
Details	PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGvAgNMAfaIgVLGgevalvgaaG

Chain	Residue	Details
A	GLY47-GLY71

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17597075

Chain	Residue	Details
A	ASP257
B	ASP257

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site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: in other chain => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM

Chain	Residue	Details
A	SER8
B	ASP12
B	GLY48
B	ASN52
B	PHE102
B	PHE116
B	GLN172
B	ASP257
A	ASP12
A	GLY48
A	ASN52
A	PHE102
A	PHE116
A	GLN172
A	ASP257
B	SER8

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM

Chain	Residue	Details
A	SER36
B	SER36

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G

Chain	Residue	Details
A	ASN195
B	ASN195

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:2PKN, ECO:0007744|PDB:4O1G

Chain	Residue	Details
A	THR223
B	THR223

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site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G

Chain	Residue	Details
A	GLY256
B	GLY256

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
A	GLY254
A	ASP257
A	VAL255
A	GLY256

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site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
B	GLY254
B	ASP257
B	VAL255
B	GLY256

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