Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FR4

Crystal structure of human serine/threonine-protein kinase 32A (YANK1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006468	biological_process	protein phosphorylation
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0035556	biological_process	intracellular signal transduction
A	0046872	molecular_function	metal ion binding
A	0106310	molecular_function	protein serine kinase activity
B	0000166	molecular_function	nucleotide binding
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006468	biological_process	protein phosphorylation
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0035556	biological_process	intracellular signal transduction
B	0046872	molecular_function	metal ion binding
B	0106310	molecular_function	protein serine kinase activity
C	0000166	molecular_function	nucleotide binding
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0006468	biological_process	protein phosphorylation
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0035556	biological_process	intracellular signal transduction
C	0046872	molecular_function	metal ion binding
C	0106310	molecular_function	protein serine kinase activity
D	0000166	molecular_function	nucleotide binding
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0006468	biological_process	protein phosphorylation
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0035556	biological_process	intracellular signal transduction
D	0046872	molecular_function	metal ion binding
D	0106310	molecular_function	protein serine kinase activity
E	0000166	molecular_function	nucleotide binding
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0006468	biological_process	protein phosphorylation
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0035556	biological_process	intracellular signal transduction
E	0046872	molecular_function	metal ion binding
E	0106310	molecular_function	protein serine kinase activity
F	0000166	molecular_function	nucleotide binding
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0005886	cellular_component	plasma membrane
F	0006468	biological_process	protein phosphorylation
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0035556	biological_process	intracellular signal transduction
F	0046872	molecular_function	metal ion binding
F	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE STU A 401

Chain	Residue
A	ILE29
A	ASP150
A	LEU153
A	THR163
A	ARG304
A	GLY30
A	LYS31
A	ALA50
A	VAL100
A	ASP101
A	LEU102
A	LEU103
A	ASP107

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 402

Chain	Residue
A	ARG27

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE STU B 401

Chain	Residue
B	ILE29
B	GLY30
B	LYS31
B	ALA50
B	LYS52
B	VAL100
B	ASP101
B	LEU102
B	LEU103
B	GLY106
B	ASP107
B	ASP150
B	ASN151
B	LEU153
B	THR163
B	ARG304
B	HOH623

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 402

Chain	Residue
B	ARG109
B	LYS148
B	ASP150
B	THR183
B	ARG221

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 403

Chain	Residue
B	GLU71
B	VAL84
B	THR163
B	ASP164
B	PHE165

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE STU C 401

Chain	Residue
C	ILE29
C	GLY30
C	LYS31
C	ALA50
C	LYS52
C	VAL100
C	ASP101
C	LEU102
C	LEU103
C	GLY106
C	ASP107
C	ASP150
C	ASN151
C	LEU153
C	THR163

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 402

Chain	Residue
C	GLN344
C	THR345
C	LEU348
F	LYS119

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 403

Chain	Residue
C	LEU102
C	LEU103
C	LYS292
C	HOH583
C	HOH585

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 404

Chain	Residue
A	SER230
A	SER231
A	HOH662
C	PHE290
C	HOH580
C	HOH584
C	HOH623
C	HOH635

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE STU D 401

Chain	Residue
D	ILE29
D	GLY30
D	ALA50
D	LYS52
D	VAL100
D	ASP101
D	LEU102
D	LEU103
D	ASP107
D	ASP150
D	LEU153
D	THR163

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE STU E 401

Chain	Residue
E	ILE29
E	GLY30
E	LYS31
E	ALA50
E	LYS52
E	VAL100
E	ASP101
E	LEU102
E	LEU103
E	ASP107
E	ASP150
E	ASN151
E	LEU153
E	THR163

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO E 402

Chain	Residue
E	LEU102
E	HOH544
E	HOH647

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE STU F 401

Chain	Residue
F	ILE29
F	GLY30
F	ALA50
F	LYS52
F	VAL100
F	ASP101
F	LEU102
F	LEU103
F	ASP107
F	ASP150
F	LEU153
F	THR163

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE29-LYS52

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

Chain	Residue	Details
A	ILE142-LEU154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1548
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q60592","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	54
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q60592","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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