3IAR

The crystal structure of human adenosine deaminase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001666	biological_process	response to hypoxia
A	0004000	molecular_function	adenosine deaminase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006154	biological_process	adenosine catabolic process
A	0006196	biological_process	AMP catabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0007155	biological_process	cell adhesion
A	0008270	molecular_function	zinc ion binding
A	0009117	biological_process	nucleotide metabolic process
A	0009168	biological_process	purine ribonucleoside monophosphate biosynthetic process
A	0009897	cellular_component	external side of plasma membrane
A	0009986	cellular_component	cell surface
A	0010035	biological_process	obsolete response to inorganic substance
A	0014074	biological_process	response to purine-containing compound
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019239	molecular_function	deaminase activity
A	0031410	cellular_component	cytoplasmic vesicle
A	0032261	biological_process	purine nucleotide salvage
A	0033632	biological_process	regulation of cell-cell adhesion mediated by integrin
A	0042110	biological_process	T cell activation
A	0043101	biological_process	purine-containing compound salvage
A	0043103	biological_process	hypoxanthine salvage
A	0045187	biological_process	regulation of circadian sleep/wake cycle, sleep
A	0046059	biological_process	dAMP catabolic process
A	0046085	biological_process	adenosine metabolic process
A	0046103	biological_process	inosine biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0046936	molecular_function	2'-deoxyadenosine deaminase activity
A	0060169	biological_process	negative regulation of adenosine receptor signaling pathway
A	0060205	cellular_component	cytoplasmic vesicle lumen
A	0070161	cellular_component	anchoring junction
A	0110148	biological_process	obsolete biomineralization

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3D1 A 501

Chain	Residue
A	NI1
A	HIS238
A	ASP295
A	ASP296
A	HOH781
A	HOH814
A	HIS17
A	ASP19
A	LEU62
A	PHE65
A	LEU106
A	GLY184
A	HIS214
A	GLU217

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI A 1

Chain	Residue
A	HIS15
A	HIS17
A	HIS214
A	ASP295
A	3D1501

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 A 371

Chain	Residue
A	LYS111
A	THR125
A	PRO126
A	ASP127
A	LYS164
A	HOH727
A	HOH1058

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NO3 A 2

Chain	Residue
A	PRO5
A	PHE7
A	ASP8
A	LYS11
A	TYR29
A	ARG33
A	GLU93
A	ASP305
A	HOH702
A	HOH827

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 372

Chain	Residue
A	PRO116
A	TRP117
A	HIS157
A	HOH397
A	HOH485
A	HOH613
A	HOH795
A	HOH797

---

Functional Information from PROSITE/UniProt

site_id	PS00485
Number of Residues	7
Details	A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP

Chain	Residue	Details
A	SER291-PRO297

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	17
Details	Region: {"description":"Required for binding to DDP4","evidences":[{"source":"PubMed","id":"15016824","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"AUG-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human adenosine deaminase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human adenosine deaminase.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3IAR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Important for interaction with adenosine receptors and increasing their affinity for agonists","evidences":[{"source":"PubMed","id":"23193172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a4l

Chain	Residue	Details
A	HIS238
A	TYR240
A	GLU217
A	ASP295

---