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

2PTX

Crystal Structure of the T. brucei enolase complexed with sulphate in closed conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0097014cellular_componentciliary plasm
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
ASER40
ASO4600
AHOH754
AHOH804
AHOH1000

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHOH798
AHOH1000
AASP243
AGLU291
AASP318
AHOH742

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AGLY38
AALA39
ASER40
AHIS156
AGLN164
ALYS343
AARG372
ASER373
AZN500
AHOH758
AHOH1000

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 700
ChainResidue
ATYR129
AGLN409
AGLU416
AHOH739
AHOH1003

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
AGLU10
ALEU411
AGLU415
AHOH807
AHOH813

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
AARG142
AGLY389
ASER390
APHE425
APRO426

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
AHIS188
ASER189
AHOH916

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKiNQIGTISEA
ChainResidueDetails
ALEU340-ALA353

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon