5E2O
FACTOR XIA IN COMPLEX WITH THE INHIBITOR 4-[(N-{(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}-L-phenylalanyl)amino]benzoic acid
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue 5JM A 301 |
Chain | Residue |
A | LEU41 |
A | ASP194 |
A | SER195 |
A | THR213 |
A | TRP215 |
A | GLY216 |
A | GLY218 |
A | CYS219 |
A | GLY226 |
A | VAL227 |
A | EDO304 |
A | HIS57 |
A | EDO308 |
A | HOH402 |
A | HOH493 |
A | TYR143 |
A | ILE151 |
A | ASP189 |
A | ALA190 |
A | CYS191 |
A | LYS192 |
A | GLY193 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | VAL23 |
A | ARG24 |
A | GLY25 |
A | GLU26 |
A | TRP27 |
A | ILE70 |
A | LEU71 |
A | LEU155 |
A | HOH412 |
A | HOH415 |
A | HOH428 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ARG170 |
A | ARG170 |
A | ARG184 |
A | ARG184 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | 5JM301 |
A | EDO308 |
A | EDO309 |
A | HOH557 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | ASN49 |
A | THR111 |
A | VAL112 |
A | GLY113 |
A | TYR114 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | GLN73 |
A | SER74 |
A | ASN153 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ARG24 |
A | SER99 |
A | LYS175 |
A | HOH456 |
A | HOH465 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue EDO A 308 |
Chain | Residue |
A | SER81 |
A | GLY216 |
A | GLU217 |
A | GLY218 |
A | 5JM301 |
A | EDO304 |
A | EDO309 |
A | HOH479 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | TRP215 |
A | GLY216 |
A | GLU217 |
A | EDO304 |
A | EDO308 |
A | HOH439 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 310 |
Chain | Residue |
A | THR177 |
A | HIS178 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 311 |
Chain | Residue |
A | SER99 |
A | GLY100 |
A | TYR101 |
A | THR177 |
A | LYS179 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 312 |
Chain | Residue |
A | VAL163 |
A | GLU167 |
A | ARG170 |
A | GLY184 |
A | TYR184 |
A | ARG184 |
A | GLU223 |
A | PRO225 |
A | HOH408 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 235 |
Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Charge relay system"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1998667","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |