5UQC

Crystal structure of mouse CRMP2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 1PG B 501

Chain	Residue
A	GLN29
B	HOH752
B	HOH905
B	ASN393
B	TYR395
B	PRO396
B	SER402
B	VAL403
B	GLY404
B	SER405
B	HOH606

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by FYN => ECO:0000250|UniProtKB:Q16555

Chain	Residue	Details
A	TYR32
B	TYR32

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337

Chain	Residue	Details
A	LYS258
B	LYS258

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942

Chain	Residue	Details
A	SER259
B	SER259

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER402
B	SER402

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455

Chain	Residue	Details
A	TYR431
B	TYR431

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:15648052

Chain	Residue	Details
A	SER465
B	SER465

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