2IUL
Human tACE g13 mutant
Functional Information from GO Data
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 | ARG186 | |
A | TYR224 | |
A | TRP485 | |
A | ARG489 |
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 | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
A | TYR523 | |
A | GLU411 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
A | GLU384 | |
A | HIS353 | |
A | HIS513 | |
A | ALA354 | |
A | TYR523 |
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 |