2W4I

Crystal structure of Helicobacter pylori glutamate racemase in complex with D-Glutamate and an inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008360	biological_process	regulation of cell shape
A	0008881	molecular_function	glutamate racemase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
A	0047661	molecular_function	amino-acid racemase activity
A	0071555	biological_process	cell wall organization
B	0008360	biological_process	regulation of cell shape
B	0008881	molecular_function	glutamate racemase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
B	0047661	molecular_function	amino-acid racemase activity
B	0071555	biological_process	cell wall organization
E	0008360	biological_process	regulation of cell shape
E	0008881	molecular_function	glutamate racemase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016853	molecular_function	isomerase activity
E	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
E	0047661	molecular_function	amino-acid racemase activity
E	0071555	biological_process	cell wall organization
F	0008360	biological_process	regulation of cell shape
F	0008881	molecular_function	glutamate racemase activity
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0016853	molecular_function	isomerase activity
F	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
F	0047661	molecular_function	amino-acid racemase activity
F	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGL A1256

Chain	Residue
A	ASP7
A	CYS181
A	THR182
A	HOH2007
A	HOH2294
A	HOH2393
A	SER8
A	PRO38
A	TYR39
A	GLY40
A	CYS70
A	ASN71
A	THR72
A	THR116

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGL B1255

Chain	Residue
B	ASP7
B	SER8
B	PRO38
B	TYR39
B	GLY40
B	CYS70
B	ASN71
B	THR72
B	THR116
B	CYS181
B	THR182
B	HOH2007
B	HOH2264
B	HOH2328

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGL E1255

Chain	Residue
E	ASP7
E	SER8
E	PRO38
E	TYR39
E	GLY40
E	CYS70
E	ASN71
E	THR72
E	THR116
E	CYS181
E	THR182
E	HIS183
E	HOH2325
E	HOH2326

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DGL F1255

Chain	Residue
F	ASP7
F	SER8
F	PRO38
F	TYR39
F	GLY40
F	CYS70
F	ASN71
F	THR72
F	THR116
F	CYS181
F	THR182
F	HOH2243
F	HOH2307

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE VGA B1256

Chain	Residue
A	PRO38
A	THR41
A	SER143
A	VAL146
A	PRO147
A	GLU150
A	GLU151
A	HOH2244
B	PRO38
B	THR41
B	LYS117
B	VAL146
B	PRO147
B	GLU150
B	GLU151
B	HOH2214
B	HOH2329

---

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE VGA E1256

Chain	Residue
E	THR41
E	SER143
E	VAL146
E	PRO147
E	GLU150
E	GLU151
E	HOH2327
E	HOH2328
F	PRO38
F	VAL146
F	PRO147
F	GLU150
F	GLU151

---

Functional Information from PROSITE/UniProt

site_id	PS00923
Number of Residues	9
Details	ASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. IVaC.NTASA

Chain	Residue	Details
A	ILE67-ALA75

---

site_id	PS00924
Number of Residues	11
Details	ASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. IIlGCTHFPlI

Chain	Residue	Details
A	ILE177-ILE187

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"O58403","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17568739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19097892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22877632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W4I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4B1F","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
A	CYS181
A	SER8
A	ASP7
A	CYS70

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
B	CYS181
B	SER8
B	ASP7
B	CYS70

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
E	CYS181
E	SER8
E	ASP7
E	CYS70

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
F	CYS181
F	SER8
F	ASP7
F	CYS70

---