4QBH

Crystal structure of a stable adenylate kinase variant AKlse5

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	43
Details	BINDING SITE FOR RESIDUE AP5 A 301

Chain	Residue
A	PRO9
A	PHE35
A	ARG36
A	MET53
A	ASP57
A	VAL59
A	THR64
A	GLY85
A	PHE86
A	ARG88
A	GLN92
A	GLY10
A	ARG123
A	ARG127
A	THR136
A	TYR137
A	HIS138
A	PHE141
A	ARG160
A	ARG171
A	GLY197
A	GLN199
A	ALA11
A	MET201
A	MG303
A	HOH403
A	HOH411
A	HOH414
A	HOH421
A	HOH438
A	HOH520
A	HOH530
A	HOH599
A	GLY12
A	HOH600
A	HOH601
A	HOH608
A	HOH619
A	LYS13
A	GLY14
A	THR15
A	THR31
A	GLY32

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	CYS130
A	CYS133
A	CYS150
A	CYS153

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 303

Chain	Residue
A	AP5301
A	HOH599
A	HOH600
A	HOH601
A	HOH602
A	HOH619

---

site_id	AC4
Number of Residues	40
Details	BINDING SITE FOR RESIDUE AP5 B 301

Chain	Residue
B	PRO9
B	GLY10
B	ALA11
B	GLY12
B	LYS13
B	GLY14
B	THR15
B	THR31
B	GLY32
B	PHE35
B	ARG36
B	MET53
B	ASP57
B	LEU58
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	MET201
B	MG303
B	HOH407
B	HOH410
B	HOH412
B	HOH414
B	HOH428
B	HOH433
B	HOH563
B	HOH564
B	HOH566

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	CYS130
B	CYS133
B	CYS150
B	CYS153

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 303

Chain	Residue
B	HOH564
B	HOH565
B	HOH566
B	AP5301
B	HOH563

---

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

---