5IUG

Crystal Structure of Anaplastic Lymphoma Kinase (ALK) in complex with 5a

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue 729 A 1501

Chain	Residue
A	ALA1148
A	MET1199
A	ALA1200
A	GLY1201
A	GLY1202
A	GLU1210
A	HIS1247
A	LEU1256
A	ILE1268
A	GLY1269
A	ASP1270
A	GLU1167
A	HOH1735
A	ILE1171
A	PHE1174
A	ILE1179
A	VAL1180
A	LEU1196
A	GLU1197
A	LEU1198

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGAFGEVYeGqvsgmpndpsplq.....VAVK

Chain	Residue	Details
A	LEU1122-LYS1150

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDIAARNCLL

Chain	Residue	Details
A	PHE1245-LEU1257

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site_id	PS00239
Number of Residues	9
Details	RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYrasYYR

Chain	Residue	Details
A	ASP1276-ARG1284

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP1249

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	GLU1197
A	HIS1124

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS1150

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:20632993

Chain	Residue	Details
A	ASP1270

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P97793

Chain	Residue	Details
A	TYR1092

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16878150, ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR1096

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR1131

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15938644

Chain	Residue	Details
A	TYR1278

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