2Q0N

Structure of human p21 activating kinase 4 (PAK4) in complex with a consensus peptide

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	4
Details	BINDING SITE FOR RESIDUE SO4 A 592

Chain	Residue
A	ARG298
A	ARG359
A	ARG360
A	GLU361

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 593

Chain	Residue
A	SEP474
A	HOH70
A	ARG359
A	LEU362
A	ASN365
A	ARG439

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 594

Chain	Residue
A	ASN413
A	GLU414

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 403

Chain	Residue
A	LYS574
A	ARG591
B	ARG-5
B	ARG-3

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 595

Chain	Residue
A	LEU475
A	LEU521
A	ARG528
A	EDO596

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 596

Chain	Residue
A	ARG528
A	EDO595

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 597

Chain	Residue
A	HOH265
A	GLU396
A	PHE397
A	LEU398
A	GLY401

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 598

Chain	Residue
A	HOH273
A	HOH275
A	GLU399
A	GLN587

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 599

Chain	Residue
A	VAL407
A	HIS409
A	THR410

---

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 => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER291

---

site_id	SWS_FT_FI5
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

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP440
A	ASP444

---

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

Chain	Residue	Details
A	ASP440
A	LYS442

---

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

Chain	Residue	Details
A	THR478
A	ASP440
A	LYS442

---

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

Chain	Residue	Details
A	SER445
A	ASP440
A	LYS442

---