3SBF

Crystal structure of the mutant P311A of enolase superfamily member from VIBRIONALES BACTERIUM complexed with Mg and D-Arabinonate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0009063	biological_process	amino acid catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0009063	biological_process	amino acid catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0009063	biological_process	amino acid catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0009063	biological_process	amino acid catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASP207
A	GLU233
A	GLU259
A	D8T404
A	HOH405

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE A 403

Chain	Residue
A	ARG384
A	TRP388
A	D8T404
A	HOH602
A	HOH610
A	HOH1138
A	HOH1415
A	ARG20
A	HIS21
A	GLN43
A	HIS209

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE D8T A 404

Chain	Residue
A	ASP207
A	HIS209
A	GLU233
A	GLU259
A	ARG280
A	HIS309
A	GLU336
A	MG402
A	EPE403
A	HOH431
A	HOH569
A	HOH763

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	ASP207
B	GLU233
B	GLU259
B	D8T404
B	HOH405

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 403

Chain	Residue
A	HOH529
B	HOH457
B	HOH498
B	HOH509
B	HOH513
B	HOH1426

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE D8T B 404

Chain	Residue
B	ASP207
B	HIS209
B	GLU233
B	GLU259
B	ARG280
B	HIS309
B	GLU336
B	MG402
B	HOH414
B	HOH632
B	HOH736

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 402

Chain	Residue
C	ASP207
C	GLU233
C	GLU259
C	D8T404
C	HOH406

---

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE C 403

Chain	Residue
C	ARG20
C	HIS21
C	HIS209
C	ARG384
C	TRP388
C	D8T404
C	HOH463
C	HOH715
C	HOH1046
C	HOH1335
C	HOH1366

---

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE D8T C 404

Chain	Residue
C	ASP207
C	HIS209
C	GLU233
C	GLU259
C	ARG280
C	HIS309
C	GLU336
C	MG402
C	EPE403
C	HOH406
C	HOH438
C	HOH1258
C	HOH1335

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 402

Chain	Residue
D	ASP207
D	GLU233
D	GLU259
D	D8T403
D	HOH404

---

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE D8T D 403

Chain	Residue
D	HIS128
D	ASP207
D	HIS209
D	GLU233
D	GLU259
D	ARG280
D	HIS309
D	ALA311
D	GLU336
D	MG402
D	HOH893
D	HOH1109

---

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiSGVDmALwDIkAKlagmPLhqLFG

Chain	Residue	Details
A	ALA91-GLY116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:24697546

Chain	Residue	Details
A	ASP207
D	ASP207
D	GLU233
D	GLU259
A	GLU233
A	GLU259
B	ASP207
B	GLU233
B	GLU259
C	ASP207
C	GLU233
C	GLU259

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0007744|PDB:3SBF

Chain	Residue	Details
A	HIS209
C	ARG280
C	HIS309
C	GLU336
D	HIS209
D	ARG280
D	HIS309
D	GLU336
A	ARG280
A	HIS309
A	GLU336
B	HIS209
B	ARG280
B	HIS309
B	GLU336
C	HIS209

---