6Q72

Crystal structure of the alanine racemase from Bacillus subtilis in the presence of only PEG 4000 and Magnesium chloride in the crystallization condition

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0006522	biological_process	alanine metabolic process
A	0008784	molecular_function	alanine racemase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030632	biological_process	D-alanine biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006522	biological_process	alanine metabolic process
B	0008784	molecular_function	alanine racemase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030632	biological_process	D-alanine biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006522	biological_process	alanine metabolic process
D	0008784	molecular_function	alanine racemase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016853	molecular_function	isomerase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030632	biological_process	D-alanine biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0005829	cellular_component	cytosol
E	0006522	biological_process	alanine metabolic process
E	0008784	molecular_function	alanine racemase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016853	molecular_function	isomerase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0030632	biological_process	D-alanine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue PLP A 401

Chain	Residue
A	LYS39
A	ILE228
A	TYR364
A	TYR43
A	LEU85
A	ARG139
A	HIS169
A	ASN209
A	THR210
A	ARG225
A	GLY227

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 402

Chain	Residue
A	ASN132
A	ARG139
A	LEU140

---

site_id	AC3
Number of Residues	3
Details	binding site for residue CL B 402

Chain	Residue
B	ASN132
B	ARG139
B	HIS169

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CL D 402

Chain	Residue
D	ASN132
D	ARG139

---

site_id	AC5
Number of Residues	3
Details	binding site for residue CL E 402

Chain	Residue
E	ASN132
E	ARG139
E	LEU140

---

site_id	AC6
Number of Residues	9
Details	binding site for Ligand PHE B 160 bound to SER B 123

Chain	Residue
B	ASN115
B	LEU118
B	GLU119
B	SER123
B	ARG126
B	LEU127
B	SER158
B	LYS159
B	LEU161

---

site_id	AC7
Number of Residues	6
Details	binding site for Ligand ALA B 124 bound to THR E 79

Chain	Residue
B	ALA122
B	SER123
B	ASN125
E	ARG74
E	THR79
E	ALA80

---

site_id	AC8
Number of Residues	19
Details	binding site for Di-peptide PLP B 401 and LYS B 39

Chain	Residue
A	MET320
A	ASP321
B	VAL37
B	VAL38
B	ALA40
B	ASN41
B	GLY42
B	TYR43
B	ALA63
B	ALA65
B	GLU69
B	ARG139
B	HIS169
B	ASN209
B	THR210
B	ARG225
B	GLY227
B	ILE228
B	TYR364

---

site_id	AC9
Number of Residues	13
Details	binding site for Di-peptide PLP B 401 and HIS B 169

Chain	Residue
B	LYS39
B	TYR43
B	ARG139
B	THR168
B	PHE170
B	GLN184
B	ASN209
B	THR210
B	ARG225
B	GLY227
B	ILE228
B	TYR364
B	CL402

---

site_id	AD1
Number of Residues	18
Details	binding site for Di-peptide PLP D 401 and LYS D 39

Chain	Residue
D	VAL37
D	VAL38
D	ALA40
D	ASN41
D	GLY42
D	TYR43
D	ALA63
D	ALA65
D	GLU69
D	LEU85
D	ARG139
D	HIS169
D	THR210
D	ARG225
D	GLY227
D	ILE228
D	TYR364
E	ASP321

---

site_id	AD2
Number of Residues	16
Details	binding site for Di-peptide ALA E 98 and ASN B 100

Chain	Residue
E	ALA97
E	TRP99
E	ILE101
E	ASN125
B	ARG74
B	LYS94
B	LYS95
B	SER96
B	ALA97
B	TRP99
B	ILE101
B	ASN125
E	ARG74
E	LYS94
E	LYS95
E	SER96

---

site_id	AD3
Number of Residues	17
Details	binding site for Di-peptide PLP E 401 and LYS E 39

Chain	Residue
D	MET320
D	ASP321
E	VAL37
E	VAL38
E	ALA40
E	ASN41
E	GLY42
E	TYR43
E	ALA63
E	ARG139
E	HIS169
E	ASN209
E	THR210
E	ARG225
E	GLY227
E	ILE228
E	TYR364

---

Functional Information from PROSITE/UniProt

site_id	PS00395
Number of Residues	11
Details	ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANGYGHG

Chain	Residue	Details
A	ALA36-GLY46

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; specific for D-alanine","evidences":[{"source":"HAMAP-Rule","id":"MF_01201","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; specific for L-alanine","evidences":[{"source":"HAMAP-Rule","id":"MF_01201","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01201","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01201","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---