4XBJ

Y274F alanine racemase from E. coli inhibited by l-ala-p

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	18
Details	binding site for residue IN5 A 401

Chain	Residue
A	LYS34
A	TYR343
A	HOH516
A	HOH530
A	HOH566
A	HOH577
B	TYR255
B	ALA302
B	MET303
B	ASP304
A	TYR38
A	ARG129
A	HIS159
A	ALA193
A	SER194
A	ARG209
A	GLY211
A	ILE212

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 402

Chain	Residue
A	LYS122
A	ARG129
A	LEU130
A	HIS159
A	HOH595

---

site_id	AC3
Number of Residues	2
Details	binding site for residue SO4 A 403

Chain	Residue
A	ARG266
B	ARG19

---

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 404

Chain	Residue
A	ARG19
B	ARG266

---

site_id	AC5
Number of Residues	17
Details	binding site for residue IN5 B 401

Chain	Residue
A	TYR255
A	ALA302
A	MET303
B	LYS34
B	TYR38
B	ARG129
B	HIS159
B	ALA193
B	SER194
B	ARG209
B	GLY211
B	ILE212
B	TYR343
B	HOH530
B	HOH538
B	HOH567
B	HOH569

---

site_id	AC6
Number of Residues	6
Details	binding site for residue SO4 B 402

Chain	Residue
B	LYS122
B	MET127
B	ARG129
B	LEU130
B	HIS159
B	HOH553

---

site_id	AC7
Number of Residues	15
Details	binding site for residue IN5 C 401

Chain	Residue
C	LYS34
C	TYR38
C	ARG129
C	HIS159
C	ALA193
C	SER194
C	ARG209
C	GLY211
C	ILE212
C	TYR343
C	HOH503
D	TYR255
D	ALA302
D	MET303
D	ASP304

---

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 C 402

Chain	Residue
C	GLU246
C	ARG266
C	HOH510

---

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 C 403

Chain	Residue
C	LYS122
C	MET127
C	ARG129
C	LEU130
C	HIS159

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 C 404

Chain	Residue
C	ARG19
D	ARG266
D	LYS317

---

site_id	AD2
Number of Residues	6
Details	binding site for residue SO4 D 401

Chain	Residue
D	TYR38
D	ALA193
D	SER194
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

---