4X8M

Crystal structure of E. coli Adenylate kinase Y171W mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004017	molecular_function	adenylate kinase activity
A	0004127	molecular_function	cytidylate kinase activity
A	0004550	molecular_function	nucleoside diphosphate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006172	biological_process	ADP biosynthetic process
A	0006225	biological_process	UDP biosynthetic process
A	0009123	biological_process	nucleoside monophosphate metabolic process
A	0009132	biological_process	nucleoside diphosphate metabolic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0015951	biological_process	purine ribonucleotide interconversion
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016740	molecular_function	transferase activity
A	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
A	0019205	molecular_function	nucleobase-containing compound kinase activity
A	0033862	molecular_function	UMP kinase activity
A	0044209	biological_process	AMP salvage
A	0046705	biological_process	CDP biosynthetic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation
A	0050145	molecular_function	nucleoside monophosphate kinase activity
A	1901566	biological_process	organonitrogen compound biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00113
Number of Residues	12
Details	ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ

Chain	Residue	Details
A	PHE81-GLN92

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733, ECO:0000269|PubMed:8451239

Chain	Residue	Details
A	GLY10
A	THR31
A	ARG36
A	LYS57
A	GLN92
A	ARG123
A	ARG156
A	LYS200

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239

Chain	Residue	Details
A	GLY85
A	ARG167

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16302237

Chain	Residue	Details
A	ARG119

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239

Chain	Residue	Details
A	VAL132

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS192

---