1ynf
From PDBWiki
Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli
| Authors | Tocilj, A. Schrag, J.D. Li, Y. Schneider, B.L. Reitzer, L. Matte, A. Cygler, M. |
| Citation | Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. PubMed |
| Release date | 2006-01-24 |
| Exp. Method | X-RAY DIFFRACTION |
| Resolution | 1.9 Å |
| Classification | HYDROLASE |
Sequence
Chain A (458 residues): Blast Uniprot EC 3.-.-.-MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNGChain B (458 residues): Blast Uniprot EC 3.-.-.-
MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNGChain C (458 residues): Blast Uniprot EC 3.-.-.-
MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNGChain D (458 residues): Blast Uniprot EC 3.-.-.-
MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNGChain E (458 residues): Blast Uniprot EC 3.-.-.-
MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNGChain F (458 residues): Blast Uniprot EC 3.-.-.-
MGSSHHHHHHGSNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKXKALADAGFPQAVIPPHERPF IPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPXWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLL KAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGXQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNP QQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFXAIEVPATQVSVSDTVSTYLFNSQL LSRDDGSXXLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESXANGGGPACLRLRVVLTEEERRAVNPAVXXNDT LFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNG
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Categories: YN | PDB entry | X-RAY DIFFRACTION | HYDROLASE | ESCHERICHIA COLI | 2006 | EC 3
