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

6NB2

CRYSTAL STRUCTURE OF ENOLASE FROM LEGIONELLA PNEUMOPHILA BOUND TO 2-PHOSPHOGLYCERIC ACID AND MAGNESIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue 2PG A 501
ChainResidue
AGLY39
AASP311
ALEU334
ALYS336
AHIS364
AARG365
ASER366
ALYS387
AMG502
AMG503
AALA40
ASER41
AHIS154
AGLN162
AGLU163
AGLU204
AASP241
AGLU284

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AASP241
AGLU284
AASP311
ALYS387
A2PG501
AHOH636

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 503
ChainResidue
ASER41
ALYS336
A2PG501
AHOH601
AHOH840

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 504
ChainResidue
AGLN135
AASP137
AARG347
AHOH609
AHOH722

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 505
ChainResidue
AGLN179
APHE230
AHOH605
AHOH608
BLYS56

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 506
ChainResidue
AARG119
ALEU129
AGLN402
AEDO507
AHOH649
AHOH806

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 507
ChainResidue
ALEU129
ATYR130
AASP376
AGLN402
AEDO506

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 501
ChainResidue
BGLN135
BASP137
BARG347
BHOH614
BHOH829

site_idAC9
Number of Residues18
Detailsbinding site for residue 2PG B 502
ChainResidue
BGLY39
BALA40
BSER41
BHIS154
BGLN162
BGLU163
BGLU204
BASP241
BGLU284
BASP311
BLEU334
BLYS336
BHIS364
BARG365
BSER366
BLYS387
BMG503
BMG504

site_idAD1
Number of Residues6
Detailsbinding site for residue MG B 503
ChainResidue
BASP241
BGLU284
BASP311
BLYS387
B2PG502
BHOH676

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 504
ChainResidue
BSER41
BLYS336
B2PG502
BHOH603
BHOH863

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO B 505
ChainResidue
ALYS56
BGLN179
BPHE230
BHOH675

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO B 506
ChainResidue
BLEU129
BASP376
BGLN402
BHOH647
BHOH857

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLSET
ChainResidueDetails
AILE333-THR346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU204
BGLU204

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS336
BLYS336

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AHIS154
BASP241
BGLU284
BASP311
BSER363
BLYS387
AGLU163
AASP241
AGLU284
AASP311
ASER363
ALYS387
BHIS154
BGLU163

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS336
BLYS336

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon