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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ZH8

A novel small molecule aPKC inhibitor

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
A	0007163	biological_process	establishment or maintenance of cell polarity
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
B	0007163	biological_process	establishment or maintenance of cell polarity
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
C	0007163	biological_process	establishment or maintenance of cell polarity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IOD A 904

Chain	Residue
A	LYS274
A	PHE297
A	ASP387
A	TYR388

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 912

Chain	Residue
A	ILE470

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE C58 A 1582

Chain	Residue
A	ASP330
A	ASP373
A	LEU376
A	THR386
A	ASP387
A	HOH2013
A	ILE251
A	VAL259
A	GLU324
A	VAL326

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1583

Chain	Residue
A	GLY422
A	PHE423
A	SER424
A	PRO492

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1584

Chain	Residue
A	MET335
A	ARG339
A	GLU436
A	GLY440

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 1585

Chain	Residue
A	SER239

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IOD C 904

Chain	Residue
C	LYS274
C	PHE297
C	ASP387
C	TYR388

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 912

Chain	Residue
C	HOH2017

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C58 C 1580

Chain	Residue
C	ILE251
C	TYR256
C	VAL259
C	GLU324
C	VAL326
C	GLY329
C	ASP330
C	ASP373
C	LEU376
C	THR386
C	ASP387

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 1581

Chain	Residue
C	LYS371
C	LEU372
C	ASP373
C	TYR410
C	GLU436

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 1582

Chain	Residue
C	CYS405
C	GLY406

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 1583

Chain	Residue
C	HIS303
C	TYR359
C	GLU362
C	GLU522

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 901

Chain	Residue
B	ASP558

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD B 904

Chain	Residue
B	LYS274
B	ASP387
B	TYR388

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 912

Chain	Residue
B	ILE470

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C58 B 1581

Chain	Residue
B	ILE251
B	GLY252
B	VAL259
B	GLU324
B	VAL326
B	ASP330
B	ASP373
B	LEU376
B	THR386
B	ASP387
B	HOH2016

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 1582

Chain	Residue
B	GLY422
B	PHE423
B	SER424
B	PRO492
B	CYS498

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 1583

Chain	Residue
B	TYR256
B	LYS371
B	ASN374

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 1584

Chain	Residue
B	MET335
B	GLU436
B	GLY440
B	ARG441

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 1585

Chain	Residue
B	ASN358
B	HIS361
B	PHE423
B	TRP427
B	GLY497

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK

Chain	Residue	Details
A	ILE251-LYS278

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

Chain	Residue	Details
A	ILE365-LEU377

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP369
B	ASP369
C	ASP369

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE251
A	LYS274
B	ILE251
B	LYS274
C	ILE251
C	LYS274

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269\|PubMed:11713277, ECO:0000269\|PubMed:11891849

Chain	Residue	Details
A	TYR256
B	TYR256
C	TYR256

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269\|PubMed:11713277

Chain	Residue	Details
A	TYR271
A	TYR325
B	TYR271
B	TYR325
C	TYR271
C	TYR325

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305\|PubMed:16125198

Chain	Residue	Details
A	TPO403
B	TPO403
C	TPO403

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:16125198, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	TPO555
B	TPO555
C	TPO555

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
A	ASP369	proton shuttle (general acid/base)
A	LYS371	electrostatic stabiliser
A	ASN374	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
B	ASP369	proton shuttle (general acid/base)
B	LYS371	electrostatic stabiliser
B	ASN374	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
C	ASP369	proton shuttle (general acid/base)
C	LYS371	electrostatic stabiliser
C	ASN374	electrostatic stabiliser

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