5LPV

Crystal structure of the BRI1 kinase domain (865-1160) in complex with AMPPNP and Mn from Arabidopsis thaliana

Replaces:  4OA9

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue ANP A 1200

Chain	Residue
A	GLY892
A	ASP1009
A	LYS1011
A	SER1013
A	ASN1014
A	LEU1016
A	ASP1027
A	MN1201
A	MN1202
A	HOH1308
A	HOH1310
A	PHE894
A	VAL897
A	ALA909
A	LYS911
A	GLU957
A	MET959
A	SER963
A	ASP966

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MN A 1201

Chain	Residue
A	ASN1014
A	ASP1027
A	ANP1200

---

site_id	AC3
Number of Residues	2
Details	binding site for residue MN A 1202

Chain	Residue
A	ASP1027
A	ANP1200

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE889-LYS912

---

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

Chain	Residue	Details
A	ILE1005-LEU1017

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP1009

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE889

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:24461462

Chain	Residue	Details
A	LYS911
A	GLU957
A	SER963
A	ASP1009
A	ASP1027

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11027724, ECO:0000269|PubMed:15894717

Chain	Residue	Details
A	ALA872

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15894717

Chain	Residue	Details
A	THR880
A	THR982

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:19105183

Chain	Residue	Details
A	SER887

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0000255

Chain	Residue	Details
A	SER891
A	SER981
A	SER1035
A	SEP1042
A	SER1060

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19124768

Chain	Residue	Details
A	TYR956

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000255

Chain	Residue	Details
A	TPO1039
A	THR1045
A	THR1049

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255

Chain	Residue	Details
A	SEP1044

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6

Chain	Residue	Details
A	TYR1052

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000255

Chain	Residue	Details
A	TYR1072

---