6BXI

X-ray crystal structure of NDR1 kinase domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue ANP A 501

Chain	Residue
A	GLY96
A	ASP173
A	ASP216
A	ASN217
A	LEU219
A	SER229
A	ASP230
A	CYS234
A	PHE410
A	MG502
A	HOH608
A	GLY98
A	HOH612
A	HOH626
A	HOH651
A	HOH681
A	HOH689
A	HOH696
A	HOH700
A	HOH705
A	HOH742
A	VAL103
A	ALA116
A	LYS118
A	VAL150
A	MET166
A	GLU167
A	LEU169

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	ASN217
A	ANP501
A	HOH700

---

site_id	AC3
Number of Residues	31
Details	binding site for residue ANP B 501

Chain	Residue
B	ILE95
B	GLY96
B	GLY98
B	VAL103
B	ALA116
B	LYS118
B	VAL150
B	MET166
B	GLU167
B	LEU169
B	ASP173
B	ASP216
B	ASN217
B	LEU219
B	SER229
B	ASP230
B	CYS234
B	PHE410
B	MG502
B	HOH615
B	HOH619
B	HOH620
B	HOH625
B	HOH628
B	HOH647
B	HOH655
B	HOH659
B	HOH663
B	HOH679
B	HOH708
B	HOH711

---

site_id	AC4
Number of Residues	4
Details	binding site for residue MG B 502

Chain	Residue
B	ASN217
B	ANP501
B	HOH620
B	HOH659

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVRlVqkkdtghv..........YAMK

Chain	Residue	Details
A	ILE95-LYS118

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDIKpdNLLL

Chain	Residue	Details
A	PHE208-LEU220

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	586
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"EMBL","id":"CAA84485.1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Motif: {"description":"UFM1-interacting motif (UFIM)","evidences":[{"source":"PubMed","id":"32537488","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O95835","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12493777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761441","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12493777","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---