5XVF

Crystal Structure of PAK4 in complex with inhibitor CZH062

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	10
Details	binding site for residue 8FR A 601

Chain	Residue
A	ILE327
A	LEU447
A	GLU329
A	ALA348
A	MET395
A	GLU396
A	LEU398
A	GLU399
A	GLY401
A	ASP444

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVCiAtvrssgklv.........AVKK

Chain	Residue	Details
A	ILE327-LYS351

---

Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	ASP440

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU

Chain	Residue	Details
A	ILE327
A	LYS350

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU

Chain	Residue	Details
A	GLU396
A	ASP458

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|Ref.32, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SEP474

---