3COG
Crystal structure of human cystathionase (Cystathionine gamma lyase) in complex with DL-propargylglycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0018272 | biological_process | protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine |
| A | 0019344 | biological_process | L-cysteine biosynthetic process |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| A | 0044524 | biological_process | protein sulfhydration |
| A | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) activity |
| A | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| A | 0098606 | molecular_function | selenocystathionine gamma-lyase activity |
| A | 1904831 | biological_process | positive regulation of aortic smooth muscle cell differentiation |
| B | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0018272 | biological_process | protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine |
| B | 0019344 | biological_process | L-cysteine biosynthetic process |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| B | 0044524 | biological_process | protein sulfhydration |
| B | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) activity |
| B | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 0098606 | molecular_function | selenocystathionine gamma-lyase activity |
| B | 1904831 | biological_process | positive regulation of aortic smooth muscle cell differentiation |
| C | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0018272 | biological_process | protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine |
| C | 0019344 | biological_process | L-cysteine biosynthetic process |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043066 | biological_process | negative regulation of apoptotic process |
| C | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| C | 0044524 | biological_process | protein sulfhydration |
| C | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) activity |
| C | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| C | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| C | 0098606 | molecular_function | selenocystathionine gamma-lyase activity |
| C | 1904831 | biological_process | positive regulation of aortic smooth muscle cell differentiation |
| D | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0018272 | biological_process | protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine |
| D | 0019344 | biological_process | L-cysteine biosynthetic process |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| D | 0044524 | biological_process | protein sulfhydration |
| D | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) activity |
| D | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| D | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| D | 0098606 | molecular_function | selenocystathionine gamma-lyase activity |
| D | 1904831 | biological_process | positive regulation of aortic smooth muscle cell differentiation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 C 606 |
| Chain | Residue |
| C | TYR114 |
| C | ASN161 |
| C | LYS212 |
| C | SER340 |
| C | LEU341 |
| C | THR355 |
| C | ARG375 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 D 607 |
| Chain | Residue |
| D | LYS212 |
| D | SER340 |
| D | LEU341 |
| D | THR355 |
| D | ARG375 |
| D | TYR114 |
| D | ASN161 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 608 |
| Chain | Residue |
| A | TYR114 |
| A | ASN161 |
| A | LYS212 |
| A | SER340 |
| A | LEU341 |
| A | THR355 |
| A | ARG375 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | SER89 |
| A | GLY90 |
| A | LEU91 |
| A | TYR114 |
| A | ASN161 |
| A | ASP187 |
| A | THR189 |
| A | SER209 |
| A | THR211 |
| A | LYS212 |
| B | TYR60 |
| B | ARG62 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 500 |
| Chain | Residue |
| C | SER89 |
| C | GLY90 |
| C | LEU91 |
| C | TYR114 |
| C | ASN161 |
| C | ASP187 |
| C | THR189 |
| C | SER209 |
| C | THR211 |
| C | LYS212 |
| D | TYR60 |
| D | ARG62 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP D 500 |
| Chain | Residue |
| C | TYR60 |
| C | ARG62 |
| D | SER89 |
| D | GLY90 |
| D | LEU91 |
| D | TYR114 |
| D | ASN161 |
| D | ASP187 |
| D | SER209 |
| D | THR211 |
| D | LYS212 |
| D | LEU341 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 2AG A 501 |
| Chain | Residue |
| A | TYR114 |
| A | ARG119 |
| A | GLU339 |
| B | TYR60 |
| B | ARG62 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 2AG C 501 |
| Chain | Residue |
| C | TYR114 |
| C | ARG119 |
| C | GLU339 |
| D | TYR60 |
| D | ARG62 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2AG D 501 |
| Chain | Residue |
| C | GLU59 |
| C | TYR60 |
| C | ARG62 |
| D | TYR114 |
| D | ARG119 |
| D | GLU339 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 601 |
| Chain | Residue |
| C | GLU127 |
| D | HIS99 |
| D | LEU100 |
| D | LEU101 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 602 |
| Chain | Residue |
| C | HIS99 |
| C | LEU100 |
| C | LEU101 |
| D | GLU127 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | HIS99 |
| A | LEU100 |
| A | LEU101 |
| B | GLU127 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 604 |
| Chain | Residue |
| B | TRP32 |
| B | THR33 |
| B | SER34 |
| D | TRP32 |
| D | THR33 |
| D | SER34 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 605 |
| Chain | Residue |
| C | LEU43 |
| C | SER248 |
| C | PRO249 |
| D | ASP219 |
| D | ASP251 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 609 |
| Chain | Residue |
| A | GLN299 |
| A | HIS300 |
| A | GLU301 |
| A | LEU302 |
| A | ARG305 |
| A | PRO295 |
| A | HIS297 |
| A | PRO298 |
Functional Information from PROSITE/UniProt
| site_id | PS00868 |
| Number of Residues | 15 |
| Details | CYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DIsmySATKYMnGHS |
| Chain | Residue | Details |
| A | ASP204-SER218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"19019829","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ASP187 | |
| A | TYR114 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ARG62 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ARG62 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | LYS212 | |
| A | SER209 | |
| A | GLN49 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | LYS212 | |
| B | SER209 | |
| B | GLN49 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | LYS212 | |
| C | SER209 | |
| C | GLN49 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | LYS212 | |
| D | SER209 | |
| D | GLN49 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | LYS212 | |
| A | ASP187 | |
| A | PHE121 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | LYS212 | |
| B | ASP187 | |
| B | PHE121 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | LYS212 | |
| C | ASP187 | |
| C | PHE121 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | LYS212 | |
| D | ASP187 | |
| D | PHE121 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ASP187 | |
| B | TYR114 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ASP187 | |
| C | TYR114 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ASP187 | |
| D | TYR114 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | LYS212 | |
| A | ASP187 | |
| A | TYR114 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | LYS212 | |
| B | ASP187 | |
| B | TYR114 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | LYS212 | |
| C | ASP187 | |
| C | TYR114 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | LYS212 | |
| D | ASP187 | |
| D | TYR114 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ARG62 |
