4QBI

Crystal structure of a stable adenylate kinase variant AKlse6

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	0005737	cellular_component	cytoplasm
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0008270	molecular_function	zinc ion binding
A	0009165	biological_process	nucleotide 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	0044209	biological_process	AMP salvage
A	0046872	molecular_function	metal ion binding
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	0005737	cellular_component	cytoplasm
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0008270	molecular_function	zinc ion binding
B	0009165	biological_process	nucleotide 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	0044209	biological_process	AMP salvage
B	0046872	molecular_function	metal ion binding
B	0046940	biological_process	nucleoside monophosphate phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	CYS130
A	CYS133
A	CYS150
A	CYS153

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	HOH678
A	AP5303
A	HOH674
A	HOH675
A	HOH676
A	HOH677

---

site_id	AC3
Number of Residues	40
Details	BINDING SITE FOR RESIDUE AP5 A 303

Chain	Residue
A	LEU8
A	PRO9
A	GLY10
A	ALA11
A	GLY12
A	LYS13
A	GLY14
A	THR15
A	THR31
A	GLY32
A	ARG36
A	MET53
A	ASP57
A	LEU58
A	VAL59
A	GLY85
A	PHE86
A	ARG88
A	GLN92
A	ARG123
A	ARG127
A	THR136
A	TYR137
A	HIS138
A	PHE141
A	ARG160
A	ARG171
A	GLY197
A	GLN199
A	ILE201
A	MG302
A	HOH413
A	HOH425
A	HOH428
A	HOH440
A	HOH483
A	HOH515
A	HOH675
A	HOH676
A	HOH678

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	CYS130
B	CYS133
B	CYS150
B	CYS153

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	AP5303
B	HOH652
B	HOH653
B	HOH654
B	HOH655

---

site_id	AC6
Number of Residues	37
Details	BINDING SITE FOR RESIDUE AP5 B 303

Chain	Residue
B	PRO9
B	GLY10
B	ALA11
B	GLY12
B	LYS13
B	GLY14
B	THR15
B	THR31
B	GLY32
B	ARG36
B	ASP57
B	VAL59
B	THR64
B	GLY85
B	PHE86
B	ARG88
B	GLN92
B	ARG123
B	ARG127
B	THR136
B	TYR137
B	HIS138
B	PHE141
B	ARG160
B	ARG171
B	GLN199
B	ILE201
B	MG302
B	HOH410
B	HOH412
B	HOH427
B	HOH437
B	HOH440
B	HOH462
B	HOH652
B	HOH654
B	HOH655

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE81-GLN92

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","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_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 290

Chain	Residue	Details
A	LYS13	electrostatic stabiliser
A	ARG88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	ARG127	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	ARG160	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	ARG171	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 290

Chain	Residue	Details
B	LYS13	electrostatic stabiliser
B	ARG88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
B	ARG127	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
B	ARG160	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
B	ARG171	electrostatic stabiliser

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