Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QK8

Crystal structure of enoyl-coA hydratase EchA15 from Mycobacterium marinum in complex with an unknown ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
D0003824molecular_functioncatalytic activity
D0004300molecular_functionenoyl-CoA hydratase activity
E0003824molecular_functioncatalytic activity
E0004300molecular_functionenoyl-CoA hydratase activity
F0003824molecular_functioncatalytic activity
F0004300molecular_functionenoyl-CoA hydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO F 297
ChainResidue
ALYS163
ATYR166
ATYR167
AHOH704
FSER186
FTHR187
FHOH601
FHOH1119
FHOH1263

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AASP103
AASN211
ATRP215
AHOH293
CEDO301

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO C 297
ChainResidue
BLYS163
BTYR166
BTYR167
CSER186
CTHR187
CHOH286
CHOH296
CHOH533
CHOH635

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BMET89
BARG93
BHOH1195
FTRP215

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
BASP103
BASN211
BTRP215
BHOH904
FEDO301

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO E 297
ChainResidue
CLYS163
CTYR166
CTYR167
ESER186
ETHR187
EHOH1101
FHOH1049

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 301
ChainResidue
ATRP215
AARG218
AEDO305
CMET89
CARG93
CHOH652

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 305
ChainResidue
AEDO269
CASP103
CASN211
CTRP215

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 297
ChainResidue
ASER186
ATHR187
AHOH284
AHOH317
AHOH623
AHOH811
DLYS163
DTYR166
DTYR167

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 301
ChainResidue
DMET89
DARG90
DARG93
DHOH1130
DHOH1142
ETRP215
EARG218

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 305
ChainResidue
DASP103
DASN211
DTRP215
DEDO269
DHOH1068

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B 297
ChainResidue
BSER186
BTHR187
BHOH391
BHOH742
BHOH871
BHOH1182
ELYS163
ETYR166
ETYR167

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D 269
ChainResidue
DTRP215
DARG218
DEDO305
EMET89
EARG93
EHOH1085

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO D 297
ChainResidue
DSER186
DTHR187
DHOH713
DHOH1165
DHOH1233
FLYS163
FTYR166
FTYR167
FHOH271

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO F 301
ChainResidue
FHOH646
BTRP215
BARG218
BEDO305
FMET89
FARG93

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL E 269
ChainResidue
EGLY70
EGLY116
EALA117

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 269
ChainResidue
AMET89
AARG90
AARG93
AHOH583
BLEU237
CTRP215
CARG218
CEDO305

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VSaIRGpavGAGlvvaLlADI
ChainResidueDetails
AVAL107-ILE127

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon