8S5M
Full-length human cystathionine beta-synthase with C-terminal 6xHis-tag, SAM bound, activated state, helical reconstruction
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 19 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM |
| Chain | Residue | Details |
| A | LYS-299-MET-281 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | CYS-355 | |
| A | HIS-342 | |
| B | CYS-355 | |
| B | HIS-342 | |
| C | CYS-355 | |
| C | HIS-342 | |
| D | CYS-355 | |
| D | HIS-342 | |
| E | CYS-355 | |
| E | HIS-342 | |
| F | CYS-355 | |
| F | HIS-342 | |
| G | CYS-355 | |
| G | HIS-342 | |
| H | CYS-355 | |
| H | HIS-342 | |
| I | CYS-355 | |
| I | HIS-342 | |
| J | CYS-355 | |
| J | HIS-342 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | ASN-258 | |
| A | GLY-151 | |
| A | SER-58 | |
| B | ASN-258 | |
| B | GLY-151 | |
| B | SER-58 | |
| C | ASN-258 | |
| C | GLY-151 | |
| C | SER-58 | |
| D | ASN-258 | |
| D | GLY-151 | |
| D | SER-58 | |
| E | ASN-258 | |
| E | GLY-151 | |
| E | SER-58 | |
| F | ASN-258 | |
| F | GLY-151 | |
| F | SER-58 | |
| G | ASN-258 | |
| G | GLY-151 | |
| G | SER-58 | |
| H | ASN-258 | |
| H | GLY-151 | |
| H | SER-58 | |
| I | ASN-258 | |
| I | GLY-151 | |
| I | SER-58 | |
| J | ASN-258 | |
| J | GLY-151 | |
| J | SER-58 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER-380 | |
| B | SER-380 | |
| C | SER-380 | |
| D | SER-380 | |
| E | SER-380 | |
| F | SER-380 | |
| G | SER-380 | |
| H | SER-380 | |
| I | SER-380 | |
| J | SER-380 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | LYS-288 | |
| B | LYS-288 | |
| C | LYS-288 | |
| D | LYS-288 | |
| E | LYS-288 | |
| F | LYS-288 | |
| G | LYS-288 | |
| H | LYS-288 | |
| I | LYS-288 | |
| J | LYS-288 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER-208 | |
| B | SER-208 | |
| C | SER-208 | |
| D | SER-208 | |
| E | SER-208 | |
| F | SER-208 | |
| G | SER-208 | |
| H | SER-208 | |
| I | SER-208 | |
| J | SER-208 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506 |
| Chain | Residue | Details |
| A | LYS-196 | |
| B | LYS-196 | |
| C | LYS-196 | |
| D | LYS-196 | |
| E | LYS-196 | |
| F | LYS-196 | |
| G | LYS-196 | |
| H | LYS-196 | |
| I | LYS-196 | |
| J | LYS-196 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| A | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| B | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| C | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| D | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| E | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| F | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA7 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| G | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA8 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| H | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA9 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| I | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA10 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| J | LYS-288 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
