1YHV

Crystal Structure of PAK1 kinase domain with two point mutations (K299R, T423E)

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 PROSITE/UniProt

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

Chain	Residue	Details
A	VAL385-LEU397

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22153498

Chain	Residue	Details
A	ASP389

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:22153498

Chain	Residue	Details
A	ILE276
A	ARG299
A	GLU345

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089

Chain	Residue	Details
A	TYR285

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945

Chain	Residue	Details
A	GLU423

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP393
A	ASP389

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS391
A	ASP389

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS391
A	ASP389
A	THR427

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS391
A	ASP389
A	ASN394

---