2ORD
Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution
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 | 0006525 | biological_process | arginine metabolic process |
A | 0006526 | biological_process | arginine biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
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 | 0006525 | biological_process | arginine metabolic process |
B | 0006526 | biological_process | arginine biosynthetic process |
B | 0008483 | molecular_function | transaminase activity |
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 | 16 |
Details | BINDING SITE FOR RESIDUE PLP A 401 |
Chain | Residue |
A | GLY94 |
A | HOH438 |
A | HOH441 |
A | HOH446 |
A | HOH458 |
A | HOH480 |
A | HOH732 |
B | THR268 |
A | THR95 |
A | PHE126 |
A | HIS127 |
A | GLU178 |
A | ASP211 |
A | GLN214 |
A | LYS240 |
A | HOH432 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP B 401 |
Chain | Residue |
A | THR268 |
A | HOH431 |
B | GLY94 |
B | THR95 |
B | ASN98 |
B | PHE126 |
B | HIS127 |
B | GLU178 |
B | ASP211 |
B | VAL213 |
B | GLN214 |
B | LYS240 |
B | HOH444 |
B | HOH452 |
B | HOH453 |
B | HOH469 |
B | HOH471 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | PHE291 |
A | LYS298 |
A | LEU364 |
A | THR365 |
A | GOL410 |
A | HOH467 |
A | HOH619 |
B | HOH588 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | ASN258 |
A | LEU260 |
A | HOH502 |
A | HOH579 |
A | HOH697 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | HIS-5 |
A | HIS-4 |
A | ALA12 |
A | THR13 |
A | ASP24 |
A | GLU25 |
A | HOH607 |
A | HOH612 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | TYR16 |
A | TYR23 |
A | HOH493 |
A | HOH660 |
B | GLU376 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 406 |
Chain | Residue |
A | SER8 |
A | ARG337 |
A | THR341 |
A | HOH722 |
A | HOH744 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 407 |
Chain | Residue |
A | TRP21 |
A | ASN346 |
A | LYS347 |
A | THR377 |
A | GOL408 |
A | HOH680 |
A | HOH710 |
B | GOL406 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 408 |
Chain | Residue |
A | GOL407 |
A | HOH710 |
B | LYS347 |
B | HOH577 |
B | HOH668 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 409 |
Chain | Residue |
A | GLU312 |
A | TYR313 |
A | HOH553 |
A | HOH724 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 410 |
Chain | Residue |
A | GLU289 |
A | PHE291 |
A | GOL402 |
A | HOH765 |
B | GLU289 |
B | GOL402 |
B | HOH468 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 411 |
Chain | Residue |
A | LYS110 |
A | GLU114 |
A | TYR117 |
A | HOH750 |
B | GLU147 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 412 |
Chain | Residue |
A | LYS228 |
A | HOH716 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 402 |
Chain | Residue |
B | LEU364 |
B | THR365 |
B | HOH450 |
A | GOL410 |
A | HOH619 |
B | PHE291 |
B | LYS298 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 403 |
Chain | Residue |
A | TRP68 |
B | HIS0 |
B | LEU3 |
B | ASN5 |
B | HOH474 |
B | HOH524 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | SER8 |
B | PHE10 |
B | ARG337 |
B | HOH580 |
B | HOH615 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 405 |
Chain | Residue |
A | GLU376 |
B | TYR16 |
B | TYR23 |
B | GLY27 |
B | HOH528 |
B | HOH689 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 406 |
Chain | Residue |
A | GLU376 |
A | THR377 |
A | GOL407 |
A | HOH707 |
B | GLY27 |
B | HOH508 |
B | HOH689 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 407 |
Chain | Residue |
A | MSE1 |
A | TYR2 |
B | SER80 |
B | GLY85 |
B | GLY86 |
B | LYS87 |
B | HOH522 |
B | HOH703 |
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.GMgRtGklfayqkygvvp....DVLttAKglgGG |
Chain | Residue | Details |
A | LEU208-GLY245 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.2, ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | GLY94 | |
B | GLY94 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|Ref.2, ECO:0000305|Ref.3 |
Chain | Residue | Details |
A | PHE126 | |
A | ASP211 | |
B | PHE126 | |
B | ASP211 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107 |
Chain | Residue | Details |
B | ARG129 | |
B | THR267 | |
A | ARG129 | |
A | THR267 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | THR268 | |
B | THR268 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107 |
Chain | Residue | Details |
A | LYS240 | |
B | LYS240 |