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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IUL

Human tACE g13 mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008241	molecular_function	peptidyl-dipeptidase activity
A	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL380-GLN389

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor 1 => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854, ECO:0000305\|PubMed:16154999, ECO:0000305\|PubMed:19773553

Chain	Residue	Details
A	TYR360

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor 1 => ECO:0000255\|PROSITE-ProRule:PRU01355

Chain	Residue	Details
A	ARG489

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton acceptor 2 => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854, ECO:0000305\|PubMed:16154999, ECO:0000305\|PubMed:19773553

Chain	Residue	Details
A	GLU384

site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: Proton donor 2 => ECO:0000255\|PROSITE-ProRule:PRU01355

Chain	Residue	Details
A	HIS513

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:16476442

Chain	Residue	Details
A	TYR200
A	PRO498

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:26403559, ECO:0007744\|PDB:2OC2, ECO:0007744\|PDB:3NXQ

Chain	Residue	Details
A	PHE359
A	LYS363

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854, ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:23056909, ECO:0007744\|PDB:4APH

Chain	Residue	Details
A	HIS387
A	HIS383

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854

Chain	Residue	Details
A	TYR224
A	TRP485
A	ARG489
A	ARG186

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854, ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:23056909, ECO:0000269\|PubMed:7961923, ECO:0007744\|PDB:4APH

Chain	Residue	Details
A	GLU411

site_id	SWS_FT_FI10
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:12540854, ECO:0000305\|PubMed:11432860

Chain	Residue	Details
A	ARG522

site_id	SWS_FT_FI11
Number of Residues	1
Details	SITE: Not glycosylated => ECO:0000269\|PubMed:20826823

Chain	Residue	Details
A	TYR492

site_id	SWS_FT_FI12
Number of Residues	1
Details	SITE: Cleavage => ECO:0000269\|PubMed:7499427, ECO:0000269\|PubMed:8253769

Chain	Residue	Details
A	ARG561

site_id	SWS_FT_FI13
Number of Residues	1
Details	SITE: Not glycosylated => ECO:0000269\|PubMed:9013598

Chain	Residue	Details
A	ASN620

site_id	SWS_FT_FI14
Number of Residues	1
Details	SITE: Cleavage => ECO:0000269\|PubMed:10769174

Chain	Residue	Details
A	ARG627

site_id	SWS_FT_FI15
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:26403559, ECO:0007744\|PDB:3NXQ

Chain	Residue	Details
A	GLU43

site_id	SWS_FT_FI16
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:9013598

Chain	Residue	Details
A	ILE80

site_id	SWS_FT_FI17
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:9013598

Chain	Residue	Details
A	ILE115

site_id	SWS_FT_FI18
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:20826823

Chain	Residue	Details
A	ALA129

site_id	SWS_FT_FI19
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16476442

Chain	Residue	Details
A	TYR287

site_id	SWS_FT_FI20
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:26403559, ECO:0007744\|PDB:3NXQ

Chain	Residue	Details
A	GLY414

site_id	SWS_FT_FI21
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:16476442, ECO:0000269\|PubMed:20826823, ECO:0000269\|PubMed:26403559, ECO:0000269\|PubMed:9013598, ECO:0007744\|PDB:3NXQ

Chain	Residue	Details
A	LYS478

site_id	SWS_FT_FI22
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:23056909, ECO:0007744\|PDB:4APH

Chain	Residue	Details
A	ASN72

site_id	SWS_FT_FI23
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:9013598

Chain	Residue	Details
A	GLN90

site_id	SWS_FT_FI24
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:23056909, ECO:0000269\|PubMed:9013598, ECO:0007744\|PDB:4APH

Chain	Residue	Details
A	ASN109

site_id	SWS_FT_FI25
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269\|PubMed:9013598

Chain	Residue	Details
A	GLN155
A	GLN337
A	GLN586

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 170

Chain	Residue	Details
A	HIS353	electrostatic stabiliser, hydrogen bond acceptor
A	ALA354	electrostatic stabiliser, hydrogen bond acceptor
A	HIS383	metal ligand
A	GLU384	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS387	metal ligand
A	GLU411	metal ligand
A	HIS513	electrostatic stabiliser, hydrogen bond donor
A	TYR523	electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-12

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