2SFP

ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	HIS166
A	ASN203
A	SER204
A	ARG219
A	GLY221
A	ILE222
A	TYR354
A	HOH512
A	HOH543
A	HOH557
B	PPI400
A	LYS39
A	TYR43
A	ARG136

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PPI B 400

Chain	Residue
A	LYS39
A	ARG136
A	TYR354
A	PLP500
B	TYR265
B	CYS311
B	MET312
B	HOH505
B	HOH582

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
A	PPI400
B	LYS39
B	TYR43
B	ARG136
B	HIS166
B	SER204
B	ARG219
B	GLY221
B	ILE222
B	TYR354
B	HOH537
B	HOH551
B	HOH581

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PPI A 400

Chain	Residue
A	TYR265
A	TYR284
A	CYS311
A	MET312
A	HOH569
A	HOH570
B	LYS39
B	ARG136
B	TYR354
B	PLP500

---

site_id	KC1
Number of Residues	1
Details	CARBAMYLATED LYSINE

Chain	Residue
A	KCX129

---

site_id	KC2
Number of Residues	1
Details	CARBAMYLATED LYSINE

Chain	Residue
B	KCX129

---

site_id	PL1
Number of Residues	1
Details	PYRIDOXAL-5-PHOSPHATE COFACTOR

Chain	Residue
A	PLP500

---

site_id	PL2
Number of Residues	1
Details	PYRIDOXAL-5-PHOSPHATE COFACTOR

Chain	Residue
B	PLP500

---

site_id	PP1
Number of Residues	1
Details	PROPIONATE INHIBITOR

Chain	Residue
B	PPI400

---

site_id	PP2
Number of Residues	1
Details	PROPIONATE INHIBITOR

Chain	Residue
A	PPI400

---

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	ALA36-GLY46

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor; specific for D-alanine","evidences":[{"source":"PubMed","id":"10502689","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor; specific for L-alanine","evidences":[{"source":"PubMed","id":"10502689","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063881","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"10079072","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12741835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2000","submissionDatabase":"PDB data bank","title":"Crystal structure of alanine racemase in complex with D-alanine phosphonate.","authors":["Stamper G.F.","Ringe D."]}}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	CYS311
A	TYR265
B	ARG136
B	LYS39

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	ARG136
A	LYS39
B	CYS311
B	TYR265

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 213

Chain	Residue	Details
A	LYS39	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	LYS140	electrostatic stabiliser
A	ALA170	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	ALA223	electrostatic stabiliser, hydrogen bond donor
A	TYR269	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	CYS315	electrostatic stabiliser
A	ILE317	electrostatic stabiliser, hydrogen bond acceptor

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 213

Chain	Residue	Details
B	LYS39	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	LYS140	electrostatic stabiliser
B	ALA170	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	ALA223	electrostatic stabiliser, hydrogen bond donor
B	TYR269	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	CYS315	electrostatic stabiliser
B	ILE317	electrostatic stabiliser, hydrogen bond acceptor

---