1ZD8

Structure of human adenylate kinase 3 like 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004017	molecular_function	AMP 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	0007596	biological_process	blood coagulation
A	0009117	biological_process	nucleotide metabolic process
A	0009123	biological_process	nucleoside monophosphate metabolic process
A	0009142	biological_process	nucleoside triphosphate 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	0016874	molecular_function	ligase activity
A	0019205	molecular_function	nucleobase-containing compound kinase activity
A	0046033	biological_process	AMP metabolic process
A	0046039	biological_process	GTP metabolic process
A	0046041	biological_process	ITP metabolic process
A	0046051	biological_process	UTP metabolic process
A	0046899	molecular_function	nucleoside triphosphate adenylate kinase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TRP86-GLN97

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	29
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"PDB data bank","title":"Structure of human adenylate kinase 3-like 1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	37
Details	Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"PDB data bank","title":"Structure of human adenylate kinase 3-like 1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32822537","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6ZJB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P08760","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","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":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS19
A	ARG127
A	ARG171
A	ARG160
A	ASP162
A	ASP163

---

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

Chain	Residue	Details
A	LYS19
A	ASP151
A	ASP39
A	ARG127

---