2C9Y

Structure of human adenylate kinase 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004017	molecular_function	adenylate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
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	0015949	biological_process	nucleobase-containing small molecule interconversion
A	0016301	molecular_function	kinase activity
A	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
A	0019205	molecular_function	nucleobase-containing compound kinase activity
A	0036126	cellular_component	sperm flagellum
A	0046033	biological_process	AMP metabolic process
A	0046034	biological_process	ATP metabolic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation
A	0070062	cellular_component	extracellular exosome
A	0097226	cellular_component	sperm mitochondrial sheath

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE B4P A1233

Chain	Residue
A	PRO24
A	PHE156
A	LYS160
A	ARG175
A	GLN214
A	THR215
A	PRO216
A	HOH2006
A	HOH2146
A	HOH2148
A	HOH2149
A	GLY25
A	HOH2150
A	ALA26
A	GLY27
A	GLY29
A	THR30
A	ARG138
A	ARG150
A	SER151

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A1234

Chain	Residue
A	LEU87
A	GLU88
A	THR89
A	LYS93
A	ARG118
A	LYS203
A	ARG204
A	HOH2079

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A1235

Chain	Residue
A	ASN38
A	ASP69
A	GLY71
A	ARG174
A	PHE220
A	HOH2013
A	HOH2151

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE96-GLN107

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|Ref.17

Chain	Residue	Details
A	GLY25
A	SER151
A	ARG175
A	GLN214

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168

Chain	Residue	Details
A	THR46
A	ARG51
A	LYS72
A	GLY100
A	GLN107
A	ARG142
A	ARG186

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|Ref.17

Chain	Residue	Details
A	ARG138

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712

Chain	Residue	Details
A	MET1

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER4
A	SER58

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP6

Chain	Residue	Details
A	LYS62
A	LYS93

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER133

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP6

Chain	Residue	Details
A	LYS181

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR195

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG175
A	ARG142
A	LYS28
A	ARG186
A	ASP177
A	ASP178

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1zio

Chain	Residue	Details
A	ARG142
A	LYS28
A	ASP48
A	ASP166

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