2VIG
Crystal structure of human short-chain acyl CoA dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
A | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005813 | cellular_component | centrosome |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
A | 0046359 | biological_process | butyrate catabolic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
B | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005813 | cellular_component | centrosome |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
B | 0046359 | biological_process | butyrate catabolic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
C | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005813 | cellular_component | centrosome |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
C | 0046359 | biological_process | butyrate catabolic process |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
D | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005813 | cellular_component | centrosome |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
D | 0046359 | biological_process | butyrate catabolic process |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
E | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0005759 | cellular_component | mitochondrial matrix |
E | 0005813 | cellular_component | centrosome |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0006635 | biological_process | fatty acid beta-oxidation |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
E | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
E | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
E | 0046359 | biological_process | butyrate catabolic process |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
F | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
F | 0005634 | cellular_component | nucleus |
F | 0005654 | cellular_component | nucleoplasm |
F | 0005739 | cellular_component | mitochondrion |
F | 0005759 | cellular_component | mitochondrial matrix |
F | 0005813 | cellular_component | centrosome |
F | 0006631 | biological_process | fatty acid metabolic process |
F | 0006635 | biological_process | fatty acid beta-oxidation |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
F | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
F | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
F | 0046359 | biological_process | butyrate catabolic process |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
G | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
G | 0005634 | cellular_component | nucleus |
G | 0005654 | cellular_component | nucleoplasm |
G | 0005739 | cellular_component | mitochondrion |
G | 0005759 | cellular_component | mitochondrial matrix |
G | 0005813 | cellular_component | centrosome |
G | 0006631 | biological_process | fatty acid metabolic process |
G | 0006635 | biological_process | fatty acid beta-oxidation |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
G | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
G | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
G | 0046359 | biological_process | butyrate catabolic process |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
H | 0004085 | molecular_function | butyryl-CoA dehydrogenase activity |
H | 0005634 | cellular_component | nucleus |
H | 0005654 | cellular_component | nucleoplasm |
H | 0005739 | cellular_component | mitochondrion |
H | 0005759 | cellular_component | mitochondrial matrix |
H | 0005813 | cellular_component | centrosome |
H | 0006631 | biological_process | fatty acid metabolic process |
H | 0006635 | biological_process | fatty acid beta-oxidation |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
H | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
H | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
H | 0046359 | biological_process | butyrate catabolic process |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | PHE152 |
A | TYR391 |
A | GLU392 |
A | THR394 |
A | GLU396 |
A | LEU400 |
A | HOH711 |
A | HOH630 |
A | HOH683 |
A | HOH633 |
A | HOH639 |
A | LEU154 |
A | HOH669 |
B | ARG297 |
B | PHE300 |
B | LEU304 |
B | LEU307 |
B | GLN365 |
B | ILE366 |
B | GLY369 |
B | HOH608 |
C | GLN308 |
A | SER155 |
A | GLY160 |
A | SER161 |
A | TRP185 |
A | THR187 |
A | LYS230 |
A | ILE387 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD B 600 |
Chain | Residue |
A | ARG297 |
A | PHE300 |
A | LEU304 |
A | LEU307 |
A | GLN365 |
A | ILE366 |
A | GLY369 |
A | HOH603 |
B | PHE152 |
B | LEU154 |
B | SER155 |
B | GLY160 |
B | SER161 |
B | TRP185 |
B | THR187 |
B | LYS230 |
B | ILE387 |
B | ILE390 |
B | TYR391 |
B | GLU392 |
B | THR394 |
B | GLU396 |
B | COS502 |
B | HOH676 |
B | HOH634 |
B | HOH681 |
B | HOH675 |
B | HOH669 |
D | GLN308 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE COS B 605 |
Chain | Residue |
A | PHE300 |
B | GLY160 |
B | SER161 |
B | PHE261 |
B | MET265 |
B | GLN266 |
B | LEU268 |
B | ASP269 |
B | ARG272 |
B | ILE342 |
B | GLU392 |
B | GLY393 |
B | ILE397 |
B | FAD501 |
B | HOH656 |
B | HOH646 |
B | HOH631 |
site_id | AC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD C 600 |
Chain | Residue |
D | PHE300 |
D | LEU304 |
D | LEU307 |
D | GLN365 |
D | ILE366 |
D | GLY369 |
D | HOH650 |
A | GLN308 |
C | PHE152 |
C | LEU154 |
C | SER155 |
C | GLY160 |
C | SER161 |
C | TRP185 |
C | THR187 |
C | LYS230 |
C | ILE387 |
C | ILE390 |
C | TYR391 |
C | GLU392 |
C | THR394 |
C | GLU396 |
C | LEU400 |
C | COS502 |
C | HOH653 |
C | HOH649 |
C | HOH625 |
C | HOH633 |
C | HOH651 |
C | HOH671 |
D | ARG297 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE COS C 605 |
Chain | Residue |
C | SER155 |
C | GLY160 |
C | SER161 |
C | LEU268 |
C | ARG272 |
C | GLU392 |
C | GLY393 |
C | ILE397 |
C | FAD501 |
site_id | AC6 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD D 600 |
Chain | Residue |
B | GLN308 |
C | ARG297 |
C | PHE300 |
C | LEU304 |
C | LEU307 |
C | VAL309 |
C | GLN365 |
C | ILE366 |
C | GLY369 |
C | HOH604 |
D | PHE152 |
D | LEU154 |
D | SER155 |
D | GLY160 |
D | SER161 |
D | TRP185 |
D | ILE186 |
D | THR187 |
D | LYS230 |
D | ILE387 |
D | TYR391 |
D | GLU392 |
D | THR394 |
D | GLU396 |
D | LEU400 |
D | COS502 |
D | HOH652 |
D | HOH645 |
D | HOH671 |
D | HOH657 |
D | HOH619 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE COS D 605 |
Chain | Residue |
D | SER155 |
D | GLY160 |
D | SER161 |
D | LEU268 |
D | ARG272 |
D | GLU392 |
D | GLY393 |
D | FAD501 |
site_id | AC8 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD E 600 |
Chain | Residue |
E | PHE152 |
E | LEU154 |
E | SER155 |
E | GLY160 |
E | SER161 |
E | TRP185 |
E | THR187 |
E | LYS230 |
E | ILE390 |
E | TYR391 |
E | GLU392 |
E | THR394 |
E | GLU396 |
E | LEU400 |
E | HOH685 |
E | HOH688 |
E | HOH616 |
E | HOH646 |
E | HOH707 |
E | HOH655 |
F | ARG297 |
F | PHE300 |
F | LEU304 |
F | LEU307 |
F | VAL309 |
F | GLN365 |
F | ILE366 |
F | GLY369 |
F | HOH604 |
G | GLN308 |
site_id | AC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD F 600 |
Chain | Residue |
E | ARG297 |
E | PHE300 |
E | LEU304 |
E | LEU307 |
E | VAL309 |
E | GLN365 |
E | ILE366 |
E | GLY369 |
E | HOH613 |
F | PHE152 |
F | LEU154 |
F | SER155 |
F | GLY160 |
F | SER161 |
F | TRP185 |
F | THR187 |
F | LYS230 |
F | TYR391 |
F | GLU392 |
F | THR394 |
F | GLU396 |
F | COS502 |
F | HOH654 |
F | HOH656 |
F | HOH647 |
F | HOH652 |
F | HOH630 |
H | GLN308 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE COS F 605 |
Chain | Residue |
F | SER155 |
F | GLY160 |
F | SER161 |
F | LEU268 |
F | ARG272 |
F | GLU392 |
F | GLY393 |
F | FAD501 |
F | HOH610 |
site_id | BC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD G 600 |
Chain | Residue |
E | GLN308 |
G | PHE152 |
G | LEU154 |
G | SER155 |
G | GLY160 |
G | SER161 |
G | TRP185 |
G | ILE186 |
G | THR187 |
G | LYS230 |
G | ILE387 |
G | ILE390 |
G | TYR391 |
G | GLU392 |
G | THR394 |
G | GLU396 |
G | LEU400 |
G | COS502 |
G | HOH637 |
G | HOH662 |
G | HOH689 |
G | HOH674 |
G | HOH630 |
H | ARG297 |
H | PHE300 |
H | LEU304 |
H | LEU307 |
H | GLN365 |
H | ILE366 |
H | GLY369 |
H | HOH644 |
site_id | BC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COS G 605 |
Chain | Residue |
G | GLY160 |
G | SER161 |
G | ALA163 |
G | ASN207 |
G | PHE261 |
G | MET265 |
G | GLN266 |
G | LEU268 |
G | ASP269 |
G | ARG272 |
G | ILE342 |
G | GLU392 |
G | GLY393 |
G | VAL401 |
G | FAD501 |
G | HOH672 |
G | HOH642 |
G | HOH601 |
G | HOH660 |
H | PHE300 |
site_id | BC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD H 600 |
Chain | Residue |
F | GLN308 |
G | ARG297 |
G | PHE300 |
G | LEU307 |
G | GLN365 |
G | ILE366 |
G | GLY369 |
G | HOH611 |
H | PHE152 |
H | LEU154 |
H | SER155 |
H | GLY160 |
H | SER161 |
H | TRP185 |
H | ILE186 |
H | THR187 |
H | LYS230 |
H | ILE387 |
H | ILE390 |
H | TYR391 |
H | GLU392 |
H | THR394 |
H | GLU396 |
H | LEU400 |
H | HOH669 |
H | HOH695 |
H | HOH647 |
H | HOH614 |
H | HOH610 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F1414 |
Chain | Residue |
F | GLN59 |
F | PRO67 |
F | GLN70 |
F | HOH699 |
F | HOH704 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO D1414 |
Chain | Residue |
D | PRO67 |
D | GLN70 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO E1414 |
Chain | Residue |
E | LEU65 |
E | PRO67 |
E | GLN70 |
E | HOH680 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO H1414 |
Chain | Residue |
H | GLN59 |
H | LEU65 |
H | PRO67 |
H | GLN70 |
H | HOH635 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B1412 |
Chain | Residue |
B | GLN59 |
B | PRO67 |
B | GLN70 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D1415 |
Chain | Residue |
B | ARG330 |
D | GLU322 |
D | ARG325 |
D | LEU326 |
D | HOH702 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A1413 |
Chain | Residue |
A | GLU322 |
A | ARG325 |
A | LEU326 |
C | ARG330 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E1415 |
Chain | Residue |
E | GLU322 |
E | ARG325 |
E | LEU326 |
G | ARG330 |
E | HOH633 |
E | HOH700 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO H1415 |
Chain | Residue |
F | ARG330 |
H | GLU322 |
H | ARG325 |
H | LEU326 |
H | HOH700 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E1416 |
Chain | Residue |
E | GLU156 |
E | PRO157 |
E | SER167 |
E | GLY181 |
E | THR182 |
E | HOH706 |
E | HOH689 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F1415 |
Chain | Residue |
D | GLU134 |
F | GLU134 |
F | GLN135 |
F | TRP139 |
F | HOH702 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO F1416 |
Chain | Residue |
F | GLU156 |
F | SER167 |
F | THR168 |
F | GLY181 |
F | THR182 |
F | HOH693 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P15651 |
Chain | Residue | Details |
A | GLU392 | |
B | GLU392 | |
C | GLU392 | |
D | GLU392 | |
E | GLU392 | |
F | GLU392 | |
G | GLU392 | |
H | GLU392 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: in other chain => ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | PHE152 | |
C | TRP185 | |
C | GLN308 | |
C | THR394 | |
D | PHE152 | |
D | TRP185 | |
D | GLN308 | |
D | THR394 | |
E | PHE152 | |
E | TRP185 | |
E | GLN308 | |
A | TRP185 | |
E | THR394 | |
F | PHE152 | |
F | TRP185 | |
F | GLN308 | |
F | THR394 | |
G | PHE152 | |
G | TRP185 | |
G | GLN308 | |
G | THR394 | |
H | PHE152 | |
A | GLN308 | |
H | TRP185 | |
H | GLN308 | |
H | THR394 | |
A | THR394 | |
B | PHE152 | |
B | TRP185 | |
B | GLN308 | |
B | THR394 | |
C | PHE152 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | SER161 | |
D | SER161 | |
D | ASP269 | |
D | GLY393 | |
E | SER161 | |
E | ASP269 | |
E | GLY393 | |
F | SER161 | |
F | ASP269 | |
F | GLY393 | |
G | SER161 | |
A | ASP269 | |
G | ASP269 | |
G | GLY393 | |
H | SER161 | |
H | ASP269 | |
H | GLY393 | |
A | GLY393 | |
B | SER161 | |
B | ASP269 | |
B | GLY393 | |
C | SER161 | |
C | ASP269 | |
C | GLY393 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ARG297 | |
E | GLN365 | |
F | ARG297 | |
F | GLN365 | |
G | ARG297 | |
G | GLN365 | |
H | ARG297 | |
H | GLN365 | |
A | GLN365 | |
B | ARG297 | |
B | GLN365 | |
C | ARG297 | |
C | GLN365 | |
D | ARG297 | |
D | GLN365 | |
E | ARG297 |
site_id | SWS_FT_FI5 |
Number of Residues | 32 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q07417 |
Chain | Residue | Details |
A | LYS51 | |
C | LYS129 | |
C | LYS262 | |
C | LYS306 | |
D | LYS51 | |
D | LYS129 | |
D | LYS262 | |
D | LYS306 | |
E | LYS51 | |
E | LYS129 | |
E | LYS262 | |
A | LYS129 | |
E | LYS306 | |
F | LYS51 | |
F | LYS129 | |
F | LYS262 | |
F | LYS306 | |
G | LYS51 | |
G | LYS129 | |
G | LYS262 | |
G | LYS306 | |
H | LYS51 | |
A | LYS262 | |
H | LYS129 | |
H | LYS262 | |
H | LYS306 | |
A | LYS306 | |
B | LYS51 | |
B | LYS129 | |
B | LYS262 | |
B | LYS306 | |
C | LYS51 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q07417 |
Chain | Residue | Details |
A | LYS72 | |
E | LYS208 | |
F | LYS72 | |
F | LYS208 | |
G | LYS72 | |
G | LYS208 | |
H | LYS72 | |
H | LYS208 | |
A | LYS208 | |
B | LYS72 | |
B | LYS208 | |
C | LYS72 | |
C | LYS208 | |
D | LYS72 | |
D | LYS208 | |
E | LYS72 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLY271 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | GLU392 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | GLU392 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | GLU392 |
site_id | CSA13 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
E | GLU392 |
site_id | CSA14 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
F | GLU392 |
site_id | CSA15 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
G | GLU392 |
site_id | CSA16 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
H | GLU392 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | GLY271 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | GLY271 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | GLY271 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
E | GLY271 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
F | GLY271 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
G | GLY271 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
H | GLY271 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLU392 |