6BAB

The structure of human CamKII with bound inhibitor

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue D0S A 401

Chain	Residue
A	LEU21
A	GLU141
A	ASN142
A	LEU144
A	ASP158
A	HOH571
A	GLY22
A	LYS23
A	VAL29
A	ALA42
A	PHE91
A	ASP92
A	VAL94
A	GLU98

---

site_id	AC2
Number of Residues	8
Details	binding site for residue TLA A 402

Chain	Residue
A	GLN119
A	ILE273
A	CYS274
A	GLN275
A	ARG276
A	SER277
A	HOH687
C	LEU301

---

site_id	AC3
Number of Residues	14
Details	binding site for residue D0S B 401

Chain	Residue
B	LEU21
B	VAL29
B	ALA42
B	PHE91
B	ASP92
B	LEU93
B	VAL94
B	GLU141
B	ASN142
B	LEU144
B	ASP158
B	HOH502
B	HOH529
B	HOH568

---

site_id	AC4
Number of Residues	8
Details	binding site for residue TLA B 402

Chain	Residue
B	GLN119
B	ILE273
B	CYS274
B	GLN275
B	ARG276
B	SER277
B	HOH534
B	HOH605

---

site_id	AC5
Number of Residues	15
Details	binding site for residue D0S C 401

Chain	Residue
C	LEU21
C	LYS23
C	VAL29
C	ALA42
C	PHE91
C	ASP92
C	LEU93
C	VAL94
C	GLY97
C	GLU98
C	GLU141
C	ASN142
C	LEU144
C	ASP158
C	HOH580

---

site_id	AC6
Number of Residues	9
Details	binding site for residue TLA C 402

Chain	Residue
A	LEU301
C	GLN119
C	ILE273
C	CYS274
C	GLN275
C	ARG276
C	SER277
C	HOH514
C	HOH522

---

site_id	AC7
Number of Residues	19
Details	binding site for residue D0S D 401

Chain	Residue
D	LEU22
D	GLY23
D	LYS24
D	VAL30
D	ALA43
D	PHE92
D	ASP93
D	LEU94
D	VAL95
D	GLY98
D	GLU142
D	ASN143
D	LEU145
D	ASP159
D	HOH504
D	HOH505
D	HOH535
D	HOH566
D	HOH643

---

site_id	AC8
Number of Residues	5
Details	binding site for Di-peptide PHE D 12 and THR D 13

Chain	Residue
C	GLN169
D	ARG11
D	ASP14
D	GLU15
D	GLU84

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU21-LYS44

---

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

Chain	Residue	Details
A	ILE133-LEU145

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP137
B	ASP137
C	ASP137
D	ASP138

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU21
A	LYS44
B	LEU21
B	LYS44
C	LEU21
C	LYS44
D	LEU22
D	LYS45

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:Q13557, ECO:0000305

Chain	Residue	Details
A	THR288
B	THR288
C	THR288
D	THR289

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