3OCE

Crystal structure of fumarate lyase:delta crystallin from Brucella melitensis bound to cobalt

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0006099	biological_process	tricarboxylic acid cycle
A	0006531	biological_process	aspartate metabolic process
A	0008797	molecular_function	aspartate ammonia-lyase activity
A	0016829	molecular_function	lyase activity
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006099	biological_process	tricarboxylic acid cycle
B	0006531	biological_process	aspartate metabolic process
B	0008797	molecular_function	aspartate ammonia-lyase activity
B	0016829	molecular_function	lyase activity
C	0003824	molecular_function	catalytic activity
C	0005829	cellular_component	cytosol
C	0006099	biological_process	tricarboxylic acid cycle
C	0006531	biological_process	aspartate metabolic process
C	0008797	molecular_function	aspartate ammonia-lyase activity
C	0016829	molecular_function	lyase activity
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006099	biological_process	tricarboxylic acid cycle
D	0006531	biological_process	aspartate metabolic process
D	0008797	molecular_function	aspartate ammonia-lyase activity
D	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO A 471

Chain	Residue
A	GLU265
A	ASP269
A	HOH476
D	GLU209

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 471

Chain	Residue
B	GLU265
B	ASP269
B	HOH483
B	HOH486
C	GLU209

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO C 471

Chain	Residue
B	GLU209
B	HOH560
C	GLU265
C	ASP269
C	HOH583

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO D 471

Chain	Residue
A	GLU209
A	HOH492
D	GLU265
D	ASP269

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO D 472

Chain	Residue
D	HIS40
D	HOH505
D	HOH509
D	HOH510

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 472

Chain	Residue
B	HIS40
B	HOH497
B	HOH498
B	HOH499
B	HOH500

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO C 472

Chain	Residue
C	HIS40

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO A 472

Chain	Residue
A	HIS40
A	HOH496
A	HOH497

---

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO B 473

Chain	Residue
B	HIS164

---

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO C 473

Chain	Residue
C	HIS164

---

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO D 473

Chain	Residue
D	HIS164

---

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO A 473

Chain	Residue
A	HIS164

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 474

Chain	Residue
C	ILE41
C	PRO42
C	ALA43
C	ARG373
C	HOH569

---

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 474

Chain	Residue
D	ALA43

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 474

Chain	Residue
B	PRO42
B	ALA43
B	ARG373

---

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 474

Chain	Residue
A	ILE41
A	PRO42
A	ALA43

---

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 475

Chain	Residue
A	GLY174

---

Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN

Chain	Residue	Details
A	GLY316-ASN325

---