3AKY

STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003688	molecular_function	DNA replication origin binding
A	0004017	molecular_function	AMP kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006172	biological_process	ADP biosynthetic process
A	0006270	biological_process	DNA replication initiation
A	0009117	biological_process	nucleotide metabolic process
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
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	0036388	biological_process	pre-replicative complex assembly
A	0046033	biological_process	AMP metabolic process
A	0046034	biological_process	ATP metabolic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	40
Details	BINDING SITE FOR RESIDUE AP5 A 301

Chain	Residue
A	PRO13
A	ARG40
A	MET57
A	GLY61
A	VAL63
A	MET68
A	GLY90
A	PHE91
A	ARG93
A	GLN97
A	ARG128
A	GLY14
A	ARG132
A	SER141
A	TYR142
A	HIS143
A	PHE146
A	ARG165
A	ARG176
A	GLN204
A	PRO205
A	PRO206
A	ALA15
A	IMD302
A	HOH501
A	HOH504
A	HOH506
A	HOH517
A	HOH530
A	HOH536
A	HOH541
A	HOH570
A	HOH587
A	GLY16
A	HOH600
A	LYS17
A	GLY18
A	THR19
A	THR35
A	GLY36

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IMD A 302

Chain	Residue
A	GLY18
A	ASP37
A	ASP89
A	AP5301
A	HOH541
A	HOH587
A	HOH621

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE86-GLN97

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	29
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	37
Details	Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594191","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594191","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1zio

Chain	Residue	Details
A	LYS17
A	ASP167
A	ARG165
A	ARG176
A	ARG132
A	ASP168

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