5OPO
Crystal structure of R238G cN-II mutant
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | GLU374 |
A | GLU378 |
A | TYR434 |
A | GLY438 |
A | HOH623 |
A | HOH627 |
A | HOH712 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | TYR475 |
A | PHE477 |
A | ARG478 |
A | HOH674 |
A | HOH710 |
A | ARG34 |
A | TYR471 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ASP252 |
A | TYR253 |
A | VAL288 |
A | ASP289 |
A | GLY310 |
A | LEU312 |
A | HOH865 |
A | HOH880 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | PHE283 |
A | ASP284 |
A | ILE286 |
A | GLN322 |
A | HIS323 |
A | GLY324 |
A | ILE325 |
A | HOH642 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | HIS276 |
A | MET432 |
A | HOH654 |
A | HOH661 |
A | HOH726 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | ARG144 |
A | LYS362 |
A | GLN453 |
A | ARG456 |
A | ARG456 |
A | TYR457 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | ALA114 |
A | TYR115 |
A | ARG144 |
A | LYS362 |
A | SER452 |
A | ARG456 |
A | ARG456 |
A | TYR457 |
A | HOH615 |
A | HOH701 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MG A 508 |
Chain | Residue |
A | ASP52 |
A | ASP54 |
A | ASP351 |
A | HOH613 |
A | HOH711 |
A | HOH908 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | ASP52 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | ASP54 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW, ECO:0007744|PDB:2XJB, ECO:0007744|PDB:2XJC, ECO:0007744|PDB:2XJD, ECO:0007744|PDB:2XJE |
Chain | Residue | Details |
A | ASP52 | |
A | ASP54 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJB |
Chain | Residue | Details |
A | ARG144 | |
A | ARG456 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJC |
Chain | Residue | Details |
A | ASN154 | |
A | LYS362 | |
A | GLN453 | |
A | TYR457 |
site_id | SWS_FT_FI6 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW |
Chain | Residue | Details |
A | ARG202 | |
A | ASP206 | |
A | LYS215 | |
A | THR249 | |
A | ASN250 | |
A | SER251 | |
A | LYS292 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM |
Chain | Residue | Details |
A | ASP351 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0007744|PDB:2JC9 |
Chain | Residue | Details |
A | MET436 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER418 |