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PDB code:

Information on SUBCLASS 11.1.1

Subclass Accession number: 150 Subclass: 11.1.1 Type: HE alpha-beta DB: ArchDB-KI

Number of loops: 19 Average sequence ID (%) : 43.2 +/- 4.7 Average RMSD (Å) : 0.57 +/- 0.20 Consensus geometry d (Å): 19 delta (°): 135-180 theta (°): 90-135 rho (°): 315-360

Loops included in this Subclass

Loop	PDB	Chain	Start	End	Sequence	Sec Struct	Ramachandran
1a06_*_115	1a06	-	115	149	ERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLY	HHHHHHHHHHHHHHHHHHHHTT---S---GGGEEE	aaaaaaaaaaaaaaaaaaaaavxbagbbbaaaxbx
1aq1_*_101	1aq1	-	101	135	LPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabbb
1b38_A_101	1b38	A	101	135	LPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI	HHHHHHHHHHHHHHHHHHHHTT---S---GGGEEE	aaaaaaaaaaaaaaaaaaaaalbbagaxbaaabbb
1bi8_A_119	1bi8	A	119	153	TETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV	HHHHHHHHHHHHHHHHHHHTTT-------TTSEEE	aaaaaaaaaaaaaaaaaaaxvlbbavaaxaaabxb
1blx_A_119	1blx	A	119	153	TETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaavbxavaxbaaabxb
1byg_A_288	1byg	A	288	322	GDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV	HHHHHHHHHHHHHHHHHHHHTT---S--SGGGEEE	aaaaaaaaaaaaaaaaaaaaavbxavaxbaaabbb
1ckp_*_101	1ckp	-	101	135	LPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaalbbae*xbaabMbb
1f3m_D_363	1f3m	D	363	397	EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL	HHHHHHHHHHHHHHHHHHHTTT------STTSEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabxb
1fgk_A_597	1fgk	A	597	631	SKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV	HHHHHHHHHHHHHHHHHHHHTT---S--SGGGEEE	aaaaaaaaaaaaaaaaaaaaavxbavaxbaaabbb
1g3n_A_119	1g3n	A	119	153	TETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV	HHHHHHHHHHHHHHHHHHHHTT---S---GGGEEE	aaaaaaaaaaaaaaaaaaaaalbbavaxbaaabxb
1hcl_*_101	1hcl	-	101	135	LPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabbb
1irk_*_1106	1irk	-	1106	1140	LQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMV	HHHHHHHHHHHHHHHHHHHHTT---S--SGGGEEE	aaaaaaaaaaaaaaaaaaaaavxbavaxbaaabbb
1jnk_*_163	1jnk	-	163	197	HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabbb
1jvp_P_101	1jvp	P	101	135	LPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI	HHHHHHHHHHHHHHHHHHHTTT---S---GGGEEE	aaaaaaaaaaaaaaaaaaaaavbbagaxbaaabbb
1p38_*_124	1p38	-	124	158	DDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAV	HHHHHHHHHHHHHHHHHHHHTT------SGGGEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabxb
1wfc_*_124	1wfc	-	124	158	DDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAV	HHHHHHHHHHHHHHHHHHHHTT-------GGGEEE	aaaaaaaaaaaaaaaaaaaaalbbaUaxbaaabbb
2fgi_A_597	2fgi	A	597	631	SKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV	HHHHHHHHHHHHHHHHHHHHTT---S--SGGGEEE	aaaaaaaaaaaaaaaaaaaaavxbagaxbaaabbb
2ptk_*_360	2ptk	-	360	394	LPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV	HHHHHHHHHHHHHHHHHHHHTT---S--STTSEEE	aaaaaaaaaaaaaaaaaaaaalbbavaxbaaabbb
2src_*_360	2src	-	360	394	LPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV	HHHHHHHHHHHHHHHHHHHHTT---S--SGGGEEE	aaaaaaaaaaaaaaaaaaaaavbbavaxbaaabbb

PDB ligands within a cut-off distance of 6 Å in this subclass

Loop	PDB	Chain	Ligands	Residue
1aq1_*_101	1aq1	*	STUSTAUROSPORINE	P - 130
1aq1_*_101	1aq1	*	STUSTAUROSPORINE	Q - 131
1aq1_*_101	1aq1	*	STUSTAUROSPORINE	N - 132
1aq1_*_101	1aq1	*	STUSTAUROSPORINE	L - 133
1aq1_*_101	1aq1	*	STUSTAUROSPORINE	L - 134
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	D - 127
1b38_A_101	1b38	A	MGMAGNESIUM ION	K - 129
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	K - 129
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	P - 130
1b38_A_101	1b38	A	MGMAGNESIUM ION	Q - 131
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	Q - 131
1b38_A_101	1b38	A	MGMAGNESIUM ION	N - 132
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	N - 132
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	L - 133
1b38_A_101	1b38	A	ATPADENOSINE-5'-TRIPHOSPHATE	L - 134

PDB Site Annotated loops in this subclass

Loop	PDB	Chain	Site	Residue
1aq1_*_101	1aq1	*	STBSTAUROSPORINE BINDING SITE.	Q - 131
1aq1_*_101	1aq1	*	STBSTAUROSPORINE BINDING SITE.	N - 132

Bibliographic annotations

Loop	PDB	Chain	Annotation	Residue
1f3m_D_363	1f3m   RefM.LEI,W.LU,W.MENG,M-C.PARRINI,M.J.ECK,B.J.MAYER,S.C.HARRISON. STRUCTURE OF PAK1 IN AN AUTOINHIBITED CONFORMATION REVEALS A MULTISTAGE ACTIVATION SWITCH  CELL (CAMBRIDGE,MASS.) v.102;387,2000	D	CATALYTIC RESIDUE	D - 389
1f3m_D_363	1f3m   RefM.LEI,W.LU,W.MENG,M-C.PARRINI,M.J.ECK,B.J.MAYER,S.C.HARRISON. STRUCTURE OF PAK1 IN AN AUTOINHIBITED CONFORMATION REVEALS A MULTISTAGE ACTIVATION SWITCH  CELL (CAMBRIDGE,MASS.) v.102;387,2000	D	CATALYTIC RESIDUE	D - 389
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ACTIVE SITE RESIDUE	L - 624
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ACTIVE SITE RESIDUE	A - 625
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ACTIVE SITE RESIDUE	A - 626
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ACTIVE SITE RESIDUE	R - 627
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ACTIVE SITE RESIDUE	N - 628
1fgk_A_597	1fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996	A	ATP BINDING RESIDUE	L - 630
2fgi_A_597	2fgi   RefM.MOHAMMADI,S.FROUM,J.M.HAMBY,M.C.SCHROEDER,R.L.PANEK,G.H.LU,A.V.ELISEENKOVA,D.GREEN,J.SCHLESSINGER,S.R.HUBBARD. CRYSTAL STRUCTURE OF AN ANGIOGENESIS INHIBITOR BOUND TO THE FGF RECEPTOR TYROSINE KINASE DOMAIN  EMBO J. v.17;5896,1998	A	ADENINE BINDING RESIDUE	L - 630

Clusters included in this Subclass

CLUSTER: HE.11.4

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