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3ZBG

Crystal structure of wild-type SCP2 thiolase from Leishmania mexicana at 1.85 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005777cellular_componentperoxisome
A0006869biological_processlipid transport
A0008289molecular_functionlipid binding
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005777cellular_componentperoxisome
B0006869biological_processlipid transport
B0008289molecular_functionlipid binding
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 1442
ChainResidue
AASN284
BMET190
BALA194
BTHR200
BMET201
BHOH2157
BHOH2299

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 1442
ChainResidue
APHE341
APRO183
ASER259

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1443
ChainResidue
BPRO183
BSER259
BMPD1451
BHOH2300

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 1443
ChainResidue
AHIS21
AILE22
ALEU220
AARG403
AHOH2015

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS B 1444
ChainResidue
BASN440
BILE441

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS B 1445
ChainResidue
AGLN75
APRO115
AMET117
AHOH2060
BILE131
BSER132

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 1444
ChainResidue
AGLY245
ATYR357

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 1445
ChainResidue
AASN216
AHIS224
ATHR225
ALYS227

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS B 1446
ChainResidue
AILE131
AHOH2104
BGLN75
BPRO115
BALA116
BMET117
BHOH2063

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 1447
ChainResidue
ATYR113
AHOH2088
BPHE312

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1448
ChainResidue
BASN234
BLYS242
BARG254
BHOH2192

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 1446
ChainResidue
APRO183
AMET255

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 1449
ChainResidue
BVAL18
BHIS63
BSER64
BGLY65
BARG175
BGLN176
BHOH2056

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 1447
ChainResidue
ALEU281
AASP285
AARG287

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS B 1450
ChainResidue
BARG315

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 1448
ChainResidue
APHE312

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD B 1451
ChainResidue
BALA158
BPHE180
BPRO183
BPHE243
BMET255
BDMS1443
BHOH2205
BHOH2301

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1452
ChainResidue
BMET255
BCYS258
BGLN260
BHOH2169

Functional Information from PROSITE/UniProt
site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NtgGGlLSfGHPvGaTG
ChainResidueDetails
AASN378-GLY394

222415

PDB entries from 2024-07-10

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