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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4XMX

Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with Bestatin

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	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0016285	molecular_function	alanyl aminopeptidase activity
A	0016787	molecular_function	hydrolase activity
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	BES902

site_id	AC2
Number of Residues	17
Details	binding site for residue BES A 902

Chain	Residue
A	ARG293
A	HIS297
A	GLU298
A	HIS301
A	LYS319
A	GLU320
A	ASN373
A	TYR376
A	TYR381
A	ZN901
A	MLI921
A	HOH1064
A	GLU121
A	ALA260
A	GLY261
A	ALA262
A	GLU264

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 903

Chain	Residue
A	SER332
A	ASP333
A	GLY335
A	HOH1410
A	HOH1482
A	HOH1576

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

Chain	Residue
A	ASP452
A	GOL910
A	MLI926
A	HOH1323
A	HOH1382
A	HOH1418

site_id	AC5
Number of Residues	6
Details	binding site for residue NA A 905

Chain	Residue
A	ARG349
A	ASP566
A	SER570
A	MLI924
A	HOH1518
A	HOH1596

site_id	AC6
Number of Residues	5
Details	binding site for residue NA A 906

Chain	Residue
A	TYR185
A	GLU264
A	GLY305
A	ASN306
A	LYS319

site_id	AC7
Number of Residues	5
Details	binding site for residue NA A 907

Chain	Residue
A	GLN19
A	ILE20
A	LEU138
A	HOH1356
A	HOH1549

site_id	AC8
Number of Residues	10
Details	binding site for residue GOL A 908

Chain	Residue
A	GLU69
A	PRO70
A	TRP71
A	THR72
A	ASP221
A	PRO224
A	ALA278
A	THR280
A	TYR288
A	HOH1103

site_id	AC9
Number of Residues	10
Details	binding site for residue GOL A 909

Chain	Residue
A	SER63
A	VAL64
A	TRP71
A	TRP74
A	ARG669
A	VAL670
A	GLU671
A	MLI918
A	MLI923
A	HOH1222

site_id	AD1
Number of Residues	9
Details	binding site for residue GOL A 910

Chain	Residue
A	ARG161
A	GLN164
A	ASP453
A	TYR454
A	NA904
A	MLI926
A	HOH1019
A	HOH1321
A	HOH1418

site_id	AD2
Number of Residues	7
Details	binding site for residue GOL A 911

Chain	Residue
A	ARG681
A	ALA707
A	ASN708
A	ASN709
A	ASP712
A	HOH1036
A	HOH1120

site_id	AD3
Number of Residues	7
Details	binding site for residue GOL A 912

Chain	Residue
A	LYS8
A	GLU123
A	ASP312
A	TRP313
A	PHE314
A	HOH1018
A	HOH1244

site_id	AD4
Number of Residues	5
Details	binding site for residue GOL A 913

Chain	Residue
A	GLN41
A	ASN67
A	PHE90
A	HOH1009
A	HOH1047

site_id	AD5
Number of Residues	6
Details	binding site for residue MLI A 914

Chain	Residue
A	THR645
A	ARG686
A	HOH1025
A	HOH1105
A	ARG641
A	GLU642

site_id	AD6
Number of Residues	9
Details	binding site for residue MLI A 915

Chain	Residue
A	GLY335
A	SER336
A	ASN340
A	HIS672
A	ILE675
A	ALA676
A	HOH1008
A	HOH1088
A	HOH1109

site_id	AD7
Number of Residues	6
Details	binding site for residue MLI A 916

Chain	Residue
A	GLU239
A	ARG240
A	PHE241
A	GLN401
A	GLN405
A	GLN585

site_id	AD8
Number of Residues	6
Details	binding site for residue MLI A 917

Chain	Residue
A	THR284
A	LYS286
A	HOH1102
A	HOH1160
A	HOH1274
A	HOH1522

site_id	AD9
Number of Residues	8
Details	binding site for residue MLI A 918

Chain	Residue
A	LEU61
A	VAL62
A	TRP74
A	ARG669
A	GLU671
A	GOL909
A	HOH1335
A	HOH1438

site_id	AE1
Number of Residues	12
Details	binding site for residue MLI A 919

Chain	Residue
A	ASN219
A	ASP256
A	ASN742
A	GLY743
A	LEU744
A	ARG781
A	HOH1004
A	HOH1007
A	HOH1115
A	HOH1205
A	HOH1324
A	HOH1357

site_id	AE2
Number of Residues	5
Details	binding site for residue MLI A 920

Chain	Residue
A	HIS11
A	GLN467
A	ARG468
A	THR469
A	GLN479

site_id	AE3
Number of Residues	6
Details	binding site for residue MLI A 921

Chain	Residue
A	TYR376
A	TYR381
A	GLU382
A	ARG825
A	BES902
A	HOH1064

site_id	AE4
Number of Residues	8
Details	binding site for residue MLI A 922

Chain	Residue
A	THR679
A	ASN682
A	ALA683
A	THR711
A	HOH1015
A	HOH1031
A	HOH1157
A	HOH1315

site_id	AE5
Number of Residues	6
Details	binding site for residue MLI A 923

Chain	Residue
A	THR72
A	TRP74
A	VAL670
A	GLU671
A	GOL909
A	HOH1252

site_id	AE6
Number of Residues	7
Details	binding site for residue MLI A 924

Chain	Residue
A	LEU532
A	TRP546
A	ASP566
A	ALA567
A	SER570
A	NA905
A	HOH1029

site_id	AE7
Number of Residues	6
Details	binding site for residue MLI A 925

Chain	Residue
A	GLN177
A	GLN549
A	GLN550
A	HOH1123
A	HOH1139
A	HOH1552

site_id	AE8
Number of Residues	9
Details	binding site for residue MLI A 926

Chain	Residue
A	ASP452
A	TYR454
A	TYR461
A	PRO528
A	GLN550
A	NA904
A	GOL910
A	HOH1001
A	HOH1323

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

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PDB entries from 2025-06-11

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