4RLG

The clear crystal structure of pyridoxal-dependent decarboxylase from sphaerobacter thermophilus dsm 20745

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016829	molecular_function	lyase activity
A	0016830	molecular_function	carbon-carbon lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
B	0005737	cellular_component	cytoplasm
B	0016829	molecular_function	lyase activity
B	0016830	molecular_function	carbon-carbon lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
C	0005737	cellular_component	cytoplasm
C	0016829	molecular_function	lyase activity
C	0016830	molecular_function	carbon-carbon lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
D	0005737	cellular_component	cytoplasm
D	0016829	molecular_function	lyase activity
D	0016830	molecular_function	carbon-carbon lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PMP A 2001

Chain	Residue
A	MSE91
A	ALA274
A	ASN301
A	GLN303
A	LLP304
A	HOH2148
A	HOH2186
A	HOH2218
B	THR351
B	HOH634
A	GLY150
A	GLY151
A	SER152
A	ASN155
A	HIS190
A	GLY245
A	THR247
A	ASP272

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 2002

Chain	Residue
A	ARG384
A	GLY388
A	GLN391
A	ARG392
A	ASP465
A	PHE468
A	HOH2361

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 2003

Chain	Residue
A	VAL389
A	ARG392
A	LEU395

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP B 501

Chain	Residue
A	THR351
B	MSE91
B	GLY150
B	GLY151
B	SER152
B	HIS190
B	GLY245
B	THR247
B	ASP272
B	ALA274
B	ASN301
B	GLN303
B	LLP304
B	HOH601
B	HOH680
B	HOH893

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 502

Chain	Residue
B	SER115
B	GLU117
B	MSE118
B	HOH754

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 503

Chain	Residue
B	ARG384
B	GLU387
B	GLY388
B	ASP465
B	PHE468
B	HOH843
B	HOH901

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B 504

Chain	Residue
B	VAL389
B	ARG392
B	LEU395

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP D 501

Chain	Residue
C	THR351
C	HOH611
D	MSE91
D	GLY150
D	GLY151
D	SER152
D	HIS190
D	GLY245
D	THR247
D	ASP272
D	ALA274
D	ASN301
D	GLN303
D	LLP304
D	HOH660
D	HOH869

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ABU D 502

Chain	Residue
D	SER186
D	ALA188
D	ALA189
D	HIS190
D	THR191

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ABU D 503

Chain	Residue
D	ALA189
D	HIS190
D	THR191
D	LEU193
D	GLN194

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 504

Chain	Residue
D	ARG384
D	GLU387
D	GLN391
D	ASP465
D	PHE468

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 505

Chain	Residue
D	VAL389
D	ARG390
D	ARG392
D	LEU395

---

site_id	BC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PMP C 501

Chain	Residue
C	GLY245
C	THR247
C	ASP272
C	ALA274
C	ASN301
C	GLN303
C	LLP304
C	HOH632
C	HOH683
C	HOH872
D	THR351
C	MSE91
C	GLY150
C	GLY151
C	SER152
C	ASN155
C	HIS190

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 502

Chain	Residue
C	ARG384
C	GLY388
C	ASP465
C	PHE468
C	HOH810

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 503

Chain	Residue
C	VAL389
C	ARG392
C	LEU395

---