3B8T

Crystal structure of Escherichia coli alaine racemase mutant P219A

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	0008360	biological_process	regulation of cell shape
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
A	0042803	molecular_function	protein homodimerization activity
A	0071555	biological_process	cell wall organization
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006522	biological_process	alanine metabolic process
B	0008360	biological_process	regulation of cell shape
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
B	0042803	molecular_function	protein homodimerization activity
B	0071555	biological_process	cell wall organization
C	0003824	molecular_function	catalytic activity
C	0005829	cellular_component	cytosol
C	0006522	biological_process	alanine metabolic process
C	0008360	biological_process	regulation of cell shape
C	0008784	molecular_function	alanine racemase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016853	molecular_function	isomerase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030632	biological_process	D-alanine biosynthetic process
C	0042803	molecular_function	protein homodimerization activity
C	0071555	biological_process	cell wall organization
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006522	biological_process	alanine metabolic process
D	0008360	biological_process	regulation of cell shape
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
D	0042803	molecular_function	protein homodimerization activity
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 360

Chain	Residue
A	ARG19
B	ARG266

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 A 361

Chain	Residue
A	ARG162

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 360

Chain	Residue
A	ARG266
B	ARG19

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 361

Chain	Residue
B	ARG162

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 360

Chain	Residue
C	ARG19
D	ARG266

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 361

Chain	Residue
C	CYS168
C	ARG162

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 362

Chain	Residue
A	TYR255
A	TYR274
A	ARG280

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLP A 1001

Chain	Residue
A	LYS34
A	TYR38
A	HIS159
A	ALA193
A	SER194
A	ARG209
A	GLY211
A	ILE212
A	TYR343

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLP B 1001

Chain	Residue
B	LYS34
B	TYR38
B	HIS159
B	ALA193
B	SER194
B	ARG209
B	GLY211
B	ILE212
B	TYR343

---

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP C 1001

Chain	Residue
C	LYS34
C	TYR38
C	LEU78
C	HIS159
C	ALA193
C	SER194
C	ARG209
C	GLY211
C	ILE212
C	TYR343

---

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLP D 1001

Chain	Residue
D	LYS34
D	TYR38
D	HIS159
D	ALA193
D	SER194
D	ARG209
D	GLY211
D	ILE212
D	TYR343

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA31-GLY41

---

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":"PubMed","id":"18434499","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"18434499","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"18434499","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	LYS34
A	ARG129

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
B	LYS34
B	ARG129

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
C	LYS34
C	ARG129

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
D	LYS34
D	ARG129

---