2AK3

THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION

Replaces:  1AK3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004017	molecular_function	AMP kinase activity
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006172	biological_process	ADP biosynthetic process
A	0009142	biological_process	nucleoside triphosphate biosynthetic process
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	0046033	biological_process	AMP metabolic process
A	0046039	biological_process	GTP metabolic process
A	0046041	biological_process	ITP metabolic process
A	0046051	biological_process	UTP metabolic process
A	0046899	molecular_function	nucleoside triphosphate adenylate kinase activity
A	0046940	biological_process	nucleoside monophosphate phosphorylation
B	0000166	molecular_function	nucleotide binding
B	0004017	molecular_function	AMP kinase activity
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006172	biological_process	ADP biosynthetic process
B	0009142	biological_process	nucleoside triphosphate biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
B	0019205	molecular_function	nucleobase-containing compound kinase activity
B	0046033	biological_process	AMP metabolic process
B	0046039	biological_process	GTP metabolic process
B	0046041	biological_process	ITP metabolic process
B	0046051	biological_process	UTP metabolic process
B	0046899	molecular_function	nucleoside triphosphate adenylate kinase activity
B	0046940	biological_process	nucleoside monophosphate phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 227

Chain	Residue
A	ALA13
A	GLY15
A	SER16
A	GLY17
A	LYS18
A	GLY19
A	HOH324

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 227

Chain	Residue
B	GLY17
B	LYS18
B	GLY19
B	HOH332
B	HOH392
B	HOH395
B	GLY15
B	SER16

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMP A 226

Chain	Residue
A	SER36
A	LEU40
A	ARG41
A	ILE58
A	LYS62
A	LEU63
A	ILE64
A	MET69
A	GLY89
A	ARG92
A	GLN96
A	HOH338
A	HOH374
A	HOH409

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AMP B 226

Chain	Residue
B	SER36
B	GLY37
B	LEU40
B	ARG41
B	ILE58
B	LYS62
B	LEU63
B	ILE64
B	MET69
B	GLY89
B	ARG92
B	GLN96
B	HOH293
B	HOH328
B	HOH330

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TRP85-GLN96

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1994037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	74
Details	Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1994037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UIJ7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"1994037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AK3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG170
A	ARG126
A	LYS18
A	ASP161
A	ARG159
A	ASP162

---

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1zio

Chain	Residue	Details
B	ARG170
B	ARG126
B	LYS18
B	ASP161
B	ARG159
B	ASP162

---