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7CLK

Mycobacterium tuberculosis enolase in complex with alternate 2-phosphoglycerate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006096biological_processglycolytic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLVKvNQIGTLTET
ChainResidueDetails
ALEU332-THR345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:37860976
ChainResidueDetails
AGLU204

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:37860976
ChainResidueDetails
ALYS335

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:6L7D, ECO:0007744|PDB:7CLK, ECO:0007744|PDB:7CLL
ChainResidueDetails
AALA41

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7E4F
ChainResidueDetails
ASER42
AGLN162

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CLL
ChainResidueDetails
AGLU163
AGLU204

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:37860976, ECO:0007744|PDB:6L7D, ECO:0007744|PDB:7CKP, ECO:0007744|PDB:7CLK, ECO:0007744|PDB:7CLL, ECO:0007744|PDB:7DLR, ECO:0007744|PDB:7E4F
ChainResidueDetails
AASP241
AASP310

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CKP
ChainResidueDetails
AGLU283

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CLK
ChainResidueDetails
AASP311

site_idSWS_FT_FI9
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7DLR, ECO:0007744|PDB:7E4F
ChainResidueDetails
ALYS335
AARG364
ASER365
ALYS386

site_idSWS_FT_FI10
Number of Residues11
DetailsMOD_RES: Glutamate methyl ester (Glu) => ECO:0000305|PubMed:37385399
ChainResidueDetails
AGLU45
AGLU406
AGLU407
AGLU47
AGLU50
AGLU73
AGLU126
AGLU195
AGLU204
AGLU367
AGLU369

site_idSWS_FT_FI11
Number of Residues7
DetailsMOD_RES: Aspartate methyl ester => ECO:0000305|PubMed:37385399
ChainResidueDetails
AASP72
AASP90
AASP123
AASP203
AASP210
AASP370
AASP375

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000305|PubMed:37385399
ChainResidueDetails
ALYS102

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:37385399
ChainResidueDetails
ASER198

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:37385399
ChainResidueDetails
ATHR199
ATHR341

222415

PDB entries from 2024-07-10

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