Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BBW

Crystal structure of human adenylate kinase 4 (AK4) in complex with diguanosine pentaphosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002082	biological_process	regulation of oxidative phosphorylation
A	0004017	molecular_function	AMP kinase activity
A	0004550	molecular_function	nucleoside diphosphate kinase activity
A	0005515	molecular_function	protein binding
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	0009117	biological_process	nucleotide metabolic process
A	0009123	biological_process	nucleoside monophosphate metabolic process
A	0009142	biological_process	nucleoside triphosphate biosynthetic process
A	0009188	biological_process	ribonucleoside diphosphate biosynthetic process
A	0015949	biological_process	nucleobase-containing small molecule interconversion
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	0036430	molecular_function	CMP kinase activity
A	0036431	molecular_function	dCMP kinase activity
A	0046033	biological_process	AMP metabolic process
A	0046034	biological_process	ATP metabolic process
A	0046039	biological_process	GTP metabolic process
A	0046899	molecular_function	nucleoside triphosphate adenylate kinase activity
A	0046940	biological_process	nucleoside monophosphate phosphorylation
A	0047506	molecular_function	dAMP kinase activity
A	0050145	molecular_function	nucleoside monophosphate kinase activity
A	0071456	biological_process	cellular response to hypoxia
B	0000166	molecular_function	nucleotide binding
B	0002082	biological_process	regulation of oxidative phosphorylation
B	0004017	molecular_function	AMP kinase activity
B	0004550	molecular_function	nucleoside diphosphate kinase activity
B	0005515	molecular_function	protein binding
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	0009117	biological_process	nucleotide metabolic process
B	0009123	biological_process	nucleoside monophosphate metabolic process
B	0009142	biological_process	nucleoside triphosphate biosynthetic process
B	0009188	biological_process	ribonucleoside diphosphate biosynthetic process
B	0015949	biological_process	nucleobase-containing small molecule interconversion
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	0036430	molecular_function	CMP kinase activity
B	0036431	molecular_function	dCMP kinase activity
B	0046033	biological_process	AMP metabolic process
B	0046034	biological_process	ATP metabolic process
B	0046039	biological_process	GTP metabolic process
B	0046899	molecular_function	nucleoside triphosphate adenylate kinase activity
B	0046940	biological_process	nucleoside monophosphate phosphorylation
B	0047506	molecular_function	dAMP kinase activity
B	0050145	molecular_function	nucleoside monophosphate kinase activity
B	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE GP5 A 225

Chain	Residue
A	PRO14
A	VAL64
A	ASP66
A	ILE69
A	GLY89
A	ARG92
A	ARG122
A	ARG126
A	ASN137
A	PHE140
A	ARG170
A	GLY15
A	GLU198
A	THR199
A	HOH238
A	HOH241
A	HOH258
A	HOH261
A	HOH266
A	HOH273
A	HOH279
A	HOH290
A	SER16
A	GLY17
A	LYS18
A	GLY19
A	THR20
A	SER36
A	LEU40

site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE GP5 B 225

Chain	Residue
B	GLY15
B	SER16
B	GLY17
B	LYS18
B	GLY19
B	THR20
B	SER36
B	LEU63
B	VAL64
B	ASP66
B	ILE69
B	GLY89
B	ARG92
B	ARG122
B	ARG126
B	VAL135
B	TYR136
B	ASN137
B	ASP139
B	PHE140
B	ARG170
B	GLU198
B	THR199
B	HOH232
B	HOH243
B	HOH248
B	HOH250
B	HOH265

Functional Information from PROSITE/UniProt

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

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_03170","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19073142","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_03170","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19073142","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03170","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of human adenylate kinase 4 (AK4) in complex with diguanosine pentaphosphate.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03170","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUR9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUR9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WUR9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)