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1ELQ

CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
B0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 1001
ChainResidue
ALEU316
AASN317
ALEU319
AVAL322

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 1002
ChainResidue
BLEU316
BASN317
BLEU319
BVAL322
BHOH1102

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 400
ChainResidue
AASN87
AVAL88
ATHR89
AHIS114
ASER164
ATRP168
AASP197
AALA199
AGLN200
AHIS222
ALYS223
AHOH1271
BTRP251
BALA275
BTHR276

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 400
ChainResidue
ATRP251
AALA275
ATHR276
BASN87
BVAL88
BTHR89
BHIS114
BTRP168
BASP197
BALA199
BGLN200
BHIS222
BLYS223
BHOH1047
BHOH1325

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDYYafTGHKwfagpaGvGgL
ChainResidueDetails
AVAL214-LEU234

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 848
ChainResidueDetails
AHIS114proton shuttle (general acid/base)
AASP197electrostatic stabiliser
AALA199electrostatic stabiliser
AGLN200electrostatic stabiliser
ALYS223covalent catalysis, proton shuttle (general acid/base)
AARG360steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 848
ChainResidueDetails
BHIS114proton shuttle (general acid/base)
BASP197electrostatic stabiliser
BALA199electrostatic stabiliser
BGLN200electrostatic stabiliser
BLYS223covalent catalysis, proton shuttle (general acid/base)
BARG360steric role

237992

PDB entries from 2025-06-25

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