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5TDE

TEV Cleaved Human ATP Citrate Lyase Bound to Citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0003824molecular_functioncatalytic activity
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue FLC A 501
ChainResidue
ASER308
AHOH676
AHOH771
B2HP901
AGLY309
ASER343
AALA345
AASN346
APHE347
ATHR348
AARG379
ANA503

site_idAC2
Number of Residues11
Detailsbinding site for residue 2HP A 502
ChainResidue
ALYS64
AARG65
AARG66
AASN203
AASP216
AHOH621
AHOH622
AHOH649
AHOH695
AHOH744
AHOH800

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
ASER308
AFLC501
AHOH620
AHOH771
B2HP901
BHOH1202

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 504
ChainResidue
AASP257
ASER260
AALA262
AHOH917

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 505
ChainResidue
ALYS58
AARG66
ALEU215
AASP216
AHOH615
AHOH657
AHOH822

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 506
ChainResidue
ATYR31
AALA32
AARG33
AHIS47

site_idAC7
Number of Residues11
Detailsbinding site for residue 2HP B 901
ChainResidue
AGLY281
AGLY282
AGLY283
AFLC501
ANA503
BSER663
BGLY664
BGLY665
BHIS760
BHOH1109
BHOH1202

site_idAC8
Number of Residues5
Detailsbinding site for residue 2HP B 902
ChainResidue
BTYR517
BHIS545
BTHR722
BHOH1005
BHOH1034

site_idAC9
Number of Residues10
Detailsbinding site for residue GOL B 903
ChainResidue
AHIS410
AHOH855
BILE673
BPHE790
BASP791
BLEU793
BGLY794
BHOH1003
BHOH1009
BHOH1084

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL B 904
ChainResidue
BLYS780
BVAL786
BPRO787
BARG788
BHOH1026
BHOH1061

Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues17
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GtcAtmfssevQFGHAG
ChainResidueDetails
BGLY746-GLY762

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGGMSnElnniisrttdGvyegVAIGGD
ChainResidueDetails
BSER661-ASP690

site_idPS01217
Number of Residues25
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GrIwtMvAGGGASvvysDtIcdl.GG
ChainResidueDetails
AGLY273-GLY297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000305|PubMed:1371749
ChainResidueDetails
BGLU770
AARG66
AGLY67
APRO109
AVAL111
AGLU118
AASP216

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
BSER789
ASER260
AALA262

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR491
AASN346
ATHR348
ATYR364
AARG379

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:23932781
ChainResidueDetails
BILE550

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:23932781, ECO:0007744|PubMed:19608861
ChainResidueDetails
BMET556
BPRO564

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER649

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BILE673

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19369195
ChainResidueDetails
BTYR692

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27664236, ECO:0000305|PubMed:23932781
ChainResidueDetails
BILE550
BMET556
BPRO564

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PDB entries from 2024-07-24

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