5MLE

Crystal Structure of Human Dihydropyrimidinease-like 2 (DPYSL2A)/Collapsin Response Mediator Protein (CRMP2 13-516) Mutant Y479E/Y499E

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PEG C 601

Chain	Residue
C	SER142
C	ASP172
C	ARG173
C	PHE174
C	GLN175
C	HOH790

---

site_id	AC2
Number of Residues	8
Details	binding site for residue EDO C 602

Chain	Residue
C	LYS398
C	GLY399
C	ARG400
C	ASP406
C	ASP408
C	PRO67
C	GLY68
C	ARG397

---

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO C 603

Chain	Residue
C	GLU221
C	HOH770

---

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO C 604

Chain	Residue
C	ASN244
C	ASN247
C	GLY271

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO C 605

Chain	Residue
C	LYS297
C	TYR431
C	ASN432
C	GLU435

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO C 606

Chain	Residue
C	ARG75
C	PHE76
C	MET78
C	ASP106
C	HIS107
C	VAL109
C	TRP123

---

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

Chain	Residue
C	MET256
C	SER282
C	THR285
C	LEU307
C	SER308
C	THR313
C	PRO314

---

site_id	AC8
Number of Residues	6
Details	binding site for residue NI C 608

Chain	Residue
C	VAL72
C	HIS73
C	HIS107
C	HIS138
C	GLN196
C	GLU277

---

site_id	AC9
Number of Residues	6
Details	binding site for residue PEG A 601

Chain	Residue
A	PHE170
A	LYS171
A	GLN209
A	ARG227
A	GLU353
A	EDO606

---

site_id	AD1
Number of Residues	9
Details	binding site for residue PEG A 602

Chain	Residue
A	GLY40
A	THR102
A	ASP134
A	LYS398
A	ASP406
A	ASP408
A	SER448
A	GLN449
A	ARG467

---

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO A 603

Chain	Residue
A	SER416
A	VAL417
A	LYS418

---

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO A 604

Chain	Residue
A	ASN244
A	ASN247
A	GLY271
A	ARG485

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO A 605

Chain	Residue
A	ASN426
C	GLU455
C	HOH785

---

site_id	AD5
Number of Residues	7
Details	binding site for residue EDO A 606

Chain	Residue
A	GLN209
A	HIS223
A	ARG227
A	PHE348
A	THR349
A	GLU353
A	PEG601

---

site_id	AD6
Number of Residues	6
Details	binding site for residue NI A 607

Chain	Residue
A	VAL72
A	HIS73
A	HIS107
A	HIS138
A	GLN196
A	GLU277

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227

Chain	Residue	Details
C	TYR32
A	TYR32

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553

Chain	Residue	Details
C	LYS258
A	LYS258

---

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

Chain	Residue	Details
C	SER259
A	SER259

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553

Chain	Residue	Details
C	TYR431
C	GLU499
A	TYR431
A	GLU499

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553

Chain	Residue	Details
C	SER465
C	SER507
A	SER465
A	SER507

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P47942

Chain	Residue	Details
C	CYS504
A	CYS504

---

site_id	SWS_FT_FI7
Number of Residues	2
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
C	THR509
A	THR509

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O08553

Chain	Residue	Details
C	THR512
A	THR512

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by GSK3-beta => ECO:0007744|PubMed:21406692

Chain	Residue	Details
C	THR514
A	THR514

---