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

3ZBK

Crystal structure of SCP2 thiolase from Leishmania mexicana: The C123A mutant.

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 DMS A 1442
ChainResidue
AGLN75
APRO115
AALA116
AMET117
BLEU128
BILE131
BCYS296

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS B 1442
ChainResidue
BPHE180
BPHE243

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 1443
ChainResidue
BVAL18
BGLY65
BARG175
BGLN176
BHOH2059

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 1443
ChainResidue
ALEU85
APHE86
ASER88
ATHR155
ATYR164
AHOH2058

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 1444
ChainResidue
BASN216
BHIS224
BLYS227

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1445
ChainResidue
BALA122
BALA123
BALA168
BGLY428
BHOH2296

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 1444
ChainResidue
ALEU228
AMET255
ATHR256

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1446
ChainResidue
ALEU128
AASN135
BGLN75
BHOH2072

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 1445
ChainResidue
AGLY245
APHE312
AARG315
AHOH2281

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1446
ChainResidue
AALA122
AALA123
AALA168
AGLY428

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

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon