Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HAK

Catalytic and ubiqutin-associated domains of MARK1/PAR-1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0004674	molecular_function	protein serine/threonine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0004674	molecular_function	protein serine/threonine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE59-LYS82

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

Chain	Residue	Details
A	ILE171-LEU183

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:Q9H0K1, ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP175
B	ASP175
C	ASP175
D	ASP175
E	ASP175
F	ASP175
G	ASP175
H	ASP175

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q9H0K1, ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE59
B	ILE59
C	ILE59
D	ILE59
E	ILE59
F	ILE59
G	ILE59
H	ILE59

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O08678, ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS82
B	LYS82
C	LYS82
D	LYS82
E	LYS82
F	LYS82
G	LYS82
H	LYS82

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:17573348

Chain	Residue	Details
A	THR201
B	THR201
C	THR201
D	THR201
E	THR201
F	THR201
G	THR201
H	THR201

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by LKB1 and TAOK1 => ECO:0000269\|PubMed:14976552

Chain	Residue	Details
A	THR208
B	THR208
C	THR208
D	THR208
E	THR208
F	THR208
G	THR208
H	THR208

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250\|UniProtKB:O08678

Chain	Residue	Details
A	SER212
B	SER212
C	SER212
D	SER212
E	SER212
F	SER212
G	SER212
H	SER212

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP175
A	GLU179

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP175
B	LYS177

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	LYS177

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	LYS177

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP175
E	LYS177

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	ASP175
F	LYS177

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
G	ASP175
G	LYS177

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
H	ASP175
H	LYS177

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	SER212
A	ASP175
A	LYS177

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	SER212
E	ASP175
E	LYS177

site_id	CSA19
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	SER212
F	ASP175
F	LYS177

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

Chain	Residue	Details
B	ASP175
B	GLU179

site_id	CSA20
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP175
A	ASN180
A	LYS177

site_id	CSA21
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP175
B	ASN180
B	LYS177

site_id	CSA22
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	ASN180
C	LYS177

site_id	CSA23
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	ASN180
D	LYS177

site_id	CSA24
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP175
E	ASN180
E	LYS177

site_id	CSA25
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	ASP175
F	ASN180
F	LYS177

site_id	CSA26
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
G	ASP175
G	ASN180
G	LYS177

site_id	CSA27
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
H	ASP175
H	ASN180
H	LYS177

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	GLU179

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	GLU179

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP175
E	GLU179

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	ASP175
F	GLU179

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
G	ASP175
G	GLU179

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
H	ASP175
H	GLU179

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP175
A	LYS177

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)