4XN5

Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Phenylalanine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 901

Chain	Residue
A	HIS297
A	HIS301
A	GLU320
A	PHE902

---

site_id	AC2
Number of Residues	14
Details	binding site for residue PHE A 902

Chain	Residue
A	GLU264
A	HIS297
A	GLU298
A	HIS301
A	GLU320
A	TYR376
A	TYR381
A	ZN901
A	HOH1414
A	GLN119
A	GLU121
A	ALA260
A	ALA262
A	MET263

---

site_id	AC3
Number of Residues	4
Details	binding site for residue NA A 903

Chain	Residue
A	GLN19
A	ILE20
A	LEU138
A	HOH1309

---

site_id	AC4
Number of Residues	6
Details	binding site for residue NA A 904

Chain	Residue
A	SER332
A	ASP333
A	GLY335
A	HOH1360
A	HOH1387
A	HOH1416

---

site_id	AC5
Number of Residues	8
Details	binding site for residue NA A 905

Chain	Residue
A	THR118
A	GLN119
A	CYS120
A	PHE187
A	ALA188
A	ASN265
A	HOH1036
A	HOH1062

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 906

Chain	Residue
A	ARG207
A	ASP246
A	ARG307
A	TYR575
A	LEU578
A	SER590
A	PRO592

---

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL A 907

Chain	Residue
A	ALA531
A	LEU532
A	TRP546
A	ASP566
A	ALA567
A	SER570

---

site_id	AC8
Number of Residues	1
Details	binding site for residue GOL A 908

Chain	Residue
A	ASP58

---

site_id	AC9
Number of Residues	3
Details	binding site for residue GOL A 909

Chain	Residue
A	ASN742
A	GLY743
A	ARG781

---

site_id	AD1
Number of Residues	10
Details	binding site for residue MLI A 910

Chain	Residue
A	SER63
A	VAL64
A	TRP71
A	TRP74
A	ARG669
A	VAL670
A	GLU671
A	MLI911
A	HOH1185
A	HOH1288

---

site_id	AD2
Number of Residues	9
Details	binding site for residue MLI A 911

Chain	Residue
A	LEU61
A	VAL62
A	SER63
A	TRP74
A	ARG669
A	GLU671
A	MLI910
A	HOH1032
A	HOH1090

---

site_id	AD3
Number of Residues	5
Details	binding site for residue MLI A 912

Chain	Residue
A	LYS8
A	GLU123
A	ASP312
A	TRP313
A	HOH1111

---

site_id	AD4
Number of Residues	6
Details	binding site for residue MLI A 913

Chain	Residue
A	TYR376
A	LEU378
A	GLU382
A	HOH1150
A	HOH1247
A	HOH1266

---

site_id	AD5
Number of Residues	10
Details	binding site for residue MLI A 914

Chain	Residue
A	GLU69
A	PRO70
A	TRP71
A	THR72
A	ASP221
A	PRO224
A	ALA278
A	THR280
A	TYR288
A	HOH1030

---

site_id	AD6
Number of Residues	4
Details	binding site for residue MLI A 915

Chain	Residue
A	ASP281
A	ASN709
A	LYS738
A	TRP739

---

site_id	AD7
Number of Residues	4
Details	binding site for residue MLI A 916

Chain	Residue
A	HOH1196
A	HOH1249
A	THR284
A	LYS286

---

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW

Chain	Residue	Details
A	VAL294-TRP303

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865

Chain	Residue	Details
A	GLU298

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	GLU121
A	GLY261
A	HIS297
A	HIS301
A	GLU320

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305

Chain	Residue	Details
A	TYR381

---