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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MKV

Crystal Structure of Human Dihydropyrimidinease-like 2 (DPYSL2A)/Collapsin Response Mediator Protein (CRMP2) residues 13-516

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
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue EDO A 601

Chain	Residue
A	LYS254
A	GLU353
A	EDO606
A	HOH800

site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 602

Chain	Residue
A	HOH728
A	ASN426
A	LEU454
A	GLY457
A	EDO603
A	HOH713

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 603

Chain	Residue
A	GLU359
A	THR424
A	EDO602
A	HOH713

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 604

Chain	Residue
A	VAL109
A	PRO110
A	GLU111
A	THR114
A	ALA119

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 605

Chain	Residue
A	ARG268
A	THR272
A	ARG481
B	SER322
B	CYS323

site_id	AC6
Number of Residues	10
Details	binding site for residue EDO A 606

Chain	Residue
A	ILE279
A	THR303
A	SER331
A	ALA332
A	CYS334
A	GLY354
A	THR355
A	EDO601
A	HOH710
A	HOH799

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO A 607

Chain	Residue
A	ARG268
A	TYR275
A	GLN327
A	PHE477
A	ARG481
A	HOH775
A	HOH822

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO A 608

Chain	Residue
A	TRP295
A	LYS345
C	LYS423
C	ARG496
C	GLY497
C	LEU498
C	TYR499

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO A 609

Chain	Residue
A	LYS345
C	TYR431
C	TYR499

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO A 610

Chain	Residue
A	ASP27
A	ASP376
A	GLN379
A	HOH716
B	PHE477

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO A 611

Chain	Residue
A	ASP476
A	LYS480
B	LYS23

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO B 601

Chain	Residue
B	HOH701
B	HOH703

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO B 602

Chain	Residue
A	SER30
A	GLU377
B	ASP476
B	LYS480
B	HOH702

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO B 603

Chain	Residue
B	ARG268
B	VAL274
B	TYR275
B	GLN327
B	ARG481

site_id	AD6
Number of Residues	9
Details	binding site for residue EDO B 604

Chain	Residue
B	ALA95
B	HIS333
B	ASN356
B	GLU359
B	GLU360
B	HIS425
B	SER427
B	ASN432
B	HOH724

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO C 601

Chain	Residue
C	ARG268
C	THR272
C	ARG481
D	HOH759

site_id	AD8
Number of Residues	1
Details	binding site for residue EDO D 601

Chain	Residue
D	HOH803

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO D 602

Chain	Residue
D	ILE401
D	ALA402

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO D 603

Chain	Residue
D	ASP27
D	ASN378
D	GLN379
D	ALA382
D	HOH819

site_id	AE2
Number of Residues	4
Details	binding site for residue EDO D 604

Chain	Residue
D	MET64
D	TRP366
D	GLU377
D	PRO414

site_id	AE3
Number of Residues	3
Details	binding site for residue EDO D 605

Chain	Residue
D	ASN426
D	LEU454
D	GLY457

site_id	AE4
Number of Residues	8
Details	binding site for residue EDO D 606

Chain	Residue
D	HIS333
D	ASN356
D	GLU359
D	GLU360
D	HIS425
D	ASN432
D	HOH703
D	HOH707

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by FYN => ECO:0000269\|PubMed:19652227

Chain	Residue	Details
A	TYR32
B	TYR32
C	TYR32
D	TYR32

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:O08553

Chain	Residue	Details
A	LYS258
B	LYS258
C	LYS258
D	LYS258

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P47942

Chain	Residue	Details
A	SER259
B	SER259
C	SER259
D	SER259

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:O08553

Chain	Residue	Details
A	TYR431
A	TYR499
B	TYR431
B	TYR499
C	TYR431
C	TYR499
D	TYR431
D	TYR499

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:O08553

Chain	Residue	Details
A	SER465
A	SER507
B	SER465
B	SER507
C	SER465
C	SER507
D	SER465
D	SER507

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000250\|UniProtKB:P47942

Chain	Residue	Details
A	CYS504
B	CYS504
C	CYS504
D	CYS504

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:10757975, ECO:0007744\|PubMed:16964243, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR509
B	THR509
C	THR509
D	THR509

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:O08553

Chain	Residue	Details
A	THR512
B	THR512
C	THR512
D	THR512

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by GSK3-beta => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
A	THR514
B	THR514
C	THR514
D	THR514

226707

PDB entries from 2024-10-30

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