4W5J

New structural conformations of adenylate kinase from Streptococcus pneumoniae D39 with Ap5A

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	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	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	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	0046940	biological_process	nucleoside monophosphate phosphorylation
C	0000166	molecular_function	nucleotide binding
C	0004017	molecular_function	AMP kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0009165	biological_process	nucleotide biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
C	0019205	molecular_function	nucleobase-containing compound kinase activity
C	0044209	biological_process	AMP salvage
C	0046940	biological_process	nucleoside monophosphate phosphorylation
D	0000166	molecular_function	nucleotide binding
D	0004017	molecular_function	AMP kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0009165	biological_process	nucleotide biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
D	0019205	molecular_function	nucleobase-containing compound kinase activity
D	0044209	biological_process	AMP salvage
D	0046940	biological_process	nucleoside monophosphate phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	AP5302
A	HOH506
A	HOH508
A	HOH512
A	HOH527

---

site_id	AC2
Number of Residues	39
Details	binding site for residue AP5 A 302

Chain	Residue
A	LYS13
A	GLY14
A	THR15
A	THR31
A	GLY32
A	PHE35
A	ARG36
A	ILE53
A	GLU57
A	VAL59
A	THR64
A	GLY86
A	TYR87
A	ARG89
A	GLN93
A	ARG124
A	ARG128
A	THR137
A	PHE138
A	HIS139
A	PHE142
A	ARG156
A	ARG167
A	GLN195
A	ILE197
A	MG301
A	HOH450
A	HOH499
A	HOH500
A	HOH501
A	HOH505
A	HOH506
A	HOH508
A	HOH521
A	HOH522
A	PRO9
A	GLY10
A	ALA11
A	GLY12

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG B 301

Chain	Residue
B	AP5302
B	HOH480
B	HOH482
B	HOH492
B	HOH497

---

site_id	AC4
Number of Residues	39
Details	binding site for residue AP5 B 302

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	ILE53
B	GLU57
B	LEU58
B	VAL59
B	THR64
B	GLY86
B	TYR87
B	ARG89
B	GLN93
B	ARG124
B	ARG128
B	THR137
B	PHE138
B	HIS139
B	PHE142
B	ARG156
B	ARG167
B	GLN195
B	ILE197
B	MG301
B	HOH439
B	HOH477
B	HOH478
B	HOH479
B	HOH480
B	HOH482
B	HOH491
B	HOH511

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG C 301

Chain	Residue
C	AP5302
C	HOH502
C	HOH510
C	HOH516
C	HOH528

---

site_id	AC6
Number of Residues	42
Details	binding site for residue AP5 C 302

Chain	Residue
C	THR15
C	THR31
C	GLY32
C	PHE35
C	ARG36
C	ILE53
C	GLU57
C	LEU58
C	VAL59
C	THR64
C	GLY86
C	TYR87
C	ARG89
C	GLN93
C	ARG124
C	ARG128
C	THR137
C	PHE138
C	HIS139
C	PHE142
C	ARG156
C	ARG167
C	GLN195
C	ILE197
C	MG301
C	HOH425
C	HOH494
C	HOH495
C	HOH496
C	HOH497
C	HOH502
C	HOH504
C	HOH510
C	HOH516
C	HOH525
C	HOH589
C	PRO9
C	GLY10
C	ALA11
C	GLY12
C	LYS13
C	GLY14

---

site_id	AC7
Number of Residues	4
Details	binding site for residue MG D 301

Chain	Residue
D	AP5302
D	HOH506
D	HOH514
D	HOH575

---

site_id	AC8
Number of Residues	40
Details	binding site for residue AP5 D 302

Chain	Residue
D	PRO9
D	GLY10
D	ALA11
D	GLY12
D	LYS13
D	GLY14
D	THR15
D	THR31
D	GLY32
D	PHE35
D	ARG36
D	ILE53
D	GLU57
D	LEU58
D	VAL59
D	THR64
D	GLY86
D	TYR87
D	ARG89
D	GLN93
D	ARG124
D	ARG128
D	THR137
D	PHE138
D	HIS139
D	PHE142
D	ARG156
D	ARG167
D	GLN195
D	ILE197
D	MG301
D	HOH430
D	HOH486
D	HOH487
D	HOH489
D	HOH490
D	HOH495
D	HOH506
D	HOH512
D	HOH531

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE82-GLN93

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	116
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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