4JEX
Y21K mutant of N-acetylornithine aminotransferase complexed with L-canaline
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006525 | biological_process | arginine metabolic process |
A | 0006526 | biological_process | arginine biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006525 | biological_process | arginine metabolic process |
B | 0006526 | biological_process | arginine biosynthetic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 501 |
Chain | Residue |
A | GLY57 |
A | HIS58 |
A | CYS59 |
A | HIS60 |
A | LEU63 |
A | GLY259 |
A | HOH608 |
B | TRP75 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | GLY50 |
A | HIS58 |
A | MET367 |
A | HOH624 |
A | HOH637 |
B | HIS76 |
B | THR77 |
B | SER78 |
B | PHE81 |
B | ACT503 |
A | ASP46 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | HIS76 |
A | THR77 |
A | SER78 |
A | PHE81 |
A | ACT504 |
A | HOH620 |
A | HOH630 |
B | ASP46 |
B | GLY50 |
B | HIS58 |
B | MET367 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | SER78 |
A | PHE81 |
A | EDO503 |
A | HOH616 |
A | HOH630 |
B | ALA48 |
B | GLY50 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 505 |
Chain | Residue |
A | THR205 |
A | PRO206 |
A | GLU207 |
A | HOH805 |
B | THR205 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 506 |
Chain | Residue |
A | TYR122 |
A | HIS127 |
A | GLN220 |
A | LEU222 |
A | EDO507 |
A | HOH685 |
A | HOH915 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | TYR122 |
A | GLU271 |
A | ACT506 |
A | HOH632 |
A | HOH655 |
A | HOH793 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
Chain | Residue |
A | SER128 |
A | ASP185 |
A | HIS186 |
A | HOH807 |
A | HOH905 |
site_id | AC9 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE P00 A 509 |
Chain | Residue |
A | SER107 |
A | GLY108 |
A | THR109 |
A | ASN112 |
A | PHE141 |
A | HIS142 |
A | GLU193 |
A | GLU198 |
A | ASP226 |
A | VAL228 |
A | GLN229 |
A | LYS255 |
A | HOH822 |
A | HOH891 |
A | HOH902 |
B | HOH783 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 510 |
Chain | Residue |
A | MET105 |
A | GLU110 |
A | GLU113 |
A | HOH738 |
A | HOH864 |
B | THR109 |
B | SER145 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 511 |
Chain | Residue |
A | LYS133 |
A | ILE168 |
A | ILE169 |
A | HIS170 |
A | HOH672 |
A | HOH691 |
A | HOH701 |
A | HOH710 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 512 |
Chain | Residue |
A | ILE94 |
A | THR97 |
A | PHE98 |
A | ALA99 |
A | HOH705 |
A | HOH917 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 501 |
Chain | Residue |
B | HIS58 |
B | CYS59 |
B | HIS60 |
B | LEU63 |
B | GLY259 |
B | HOH628 |
A | TRP75 |
B | GLY57 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 502 |
Chain | Residue |
A | THR205 |
B | THR205 |
B | PRO206 |
B | GLU207 |
B | HOH855 |
B | HOH889 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 503 |
Chain | Residue |
A | ALA48 |
A | GLY50 |
A | LEU369 |
A | EDO502 |
A | HOH637 |
B | SER78 |
B | PHE81 |
B | HOH706 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 504 |
Chain | Residue |
A | VAL80 |
B | ALA22 |
B | PRO23 |
B | PHE26 |
B | TYR359 |
B | ALA362 |
B | HOH618 |
B | HOH881 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 505 |
Chain | Residue |
B | GLU345 |
B | LEU346 |
B | LYS347 |
B | LYS351 |
B | ASP374 |
B | HOH744 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 506 |
Chain | Residue |
B | TYR122 |
B | GLU271 |
B | HOH651 |
B | HOH713 |
B | HOH912 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT B 507 |
Chain | Residue |
A | THR109 |
A | SER145 |
B | MET105 |
B | GLU110 |
B | GLU113 |
B | HOH783 |
B | HOH910 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TNF B 508 |
Chain | Residue |
A | LYS30 |
A | TRP37 |
A | GLU43 |
B | LEU18 |
B | PRO19 |
B | VAL20 |
B | LYS21 |
B | ARG355 |
B | TYR359 |
B | HOH837 |
B | HOH876 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT B 509 |
Chain | Residue |
B | LYS133 |
B | ILE168 |
B | HIS170 |
B | HOH667 |
B | HOH671 |
B | HOH679 |
B | HOH812 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 510 |
Chain | Residue |
A | VAL80 |
B | ASN370 |
B | ARG377 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA B 511 |
Chain | Residue |
B | ILE94 |
B | THR97 |
B | PHE98 |
B | ALA99 |
B | HOH716 |
B | HOH726 |
B | HOH914 |
site_id | CC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE P00 B 512 |
Chain | Residue |
A | HOH738 |
B | SER107 |
B | GLY108 |
B | THR109 |
B | ASN112 |
B | PHE141 |
B | HIS142 |
B | GLU193 |
B | ASP226 |
B | VAL228 |
B | GLN229 |
B | LYS255 |
B | HOH738 |
B | HOH745 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVqc.GMgRtGdlfaymhygvtp....DILtsAKalgGG |
Chain | Residue | Details |
A | LEU223-GLY260 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:17680699 |
Chain | Residue | Details |
B | GLY108 | |
B | THR284 | |
A | GLY108 | |
A | THR284 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|PubMed:17680699 |
Chain | Residue | Details |
A | PHE141 | |
A | ASP226 | |
B | PHE141 | |
B | ASP226 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107 |
Chain | Residue | Details |
B | ARG144 | |
B | SER283 | |
A | ARG144 | |
A | SER283 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:17680699 |
Chain | Residue | Details |
A | LYS255 | |
B | LYS255 |