5JBB
Crystal structure of factor IXa variant V16I K98T Y177T I213V in complex with EGR-chloromethylketone
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA S 301 |
Chain | Residue |
S | GLU70 |
S | ASN72 |
S | GLU75 |
S | GLU77 |
S | GLU80 |
S | HOH434 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue 0GJ S 302 |
Chain | Residue |
S | SER190 |
S | CYS191 |
S | GLN192 |
S | GLY193 |
S | SER195 |
S | SER214 |
S | TRP215 |
S | GLY216 |
S | GLU219 |
S | GLY226 |
S | HOH403 |
S | HOH450 |
S | HOH521 |
S | HOH526 |
S | HOH529 |
S | HIS57 |
S | TYR99 |
S | ASP189 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue DMS S 303 |
Chain | Residue |
S | ASP21 |
S | ARG150 |
S | ALA152 |
S | LEU153 |
S | VAL154 |
S | GLN156 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
Chain | Residue | Details |
S | VAL53-CYS58 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV |
Chain | Residue | Details |
S | ASP189-VAL200 |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CsCteGYrlaenqksC |
Chain | Residue | Details |
E | CYS109-CYS124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613 |
Chain | Residue | Details |
S | HIS57 | |
S | SER195 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:659613 |
Chain | Residue | Details |
S | ASP102 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5 |
Chain | Residue | Details |
S | GLU70 | |
S | ASN72 | |
S | GLU75 | |
S | GLU77 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5 |
Chain | Residue | Details |
S | GLU80 |