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7LA1

Crystal structure of phosphoglycerate kinase from Mycobacterium avium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0043531molecular_functionADP binding
B0000166molecular_functionnucleotide binding
B0004618molecular_functionphosphoglycerate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0043531molecular_functionADP binding
C0000166molecular_functionnucleotide binding
C0004618molecular_functionphosphoglycerate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0043531molecular_functionADP binding
D0000166molecular_functionnucleotide binding
D0004618molecular_functionphosphoglycerate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0043531molecular_functionADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue EDO A 501
ChainResidue
ALYS133
AASP134
AASP135
AHOH625
AHOH631
AHOH633
AHOH651
AHOH701

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 502
ChainResidue
ASER210
AGLY233
AGLY234
AHOH658
AHOH905
AGLY209

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 503
ChainResidue
AARG69
APRO70
AARG125
AASP127
AALA128
ATHR131
AHOH753
AHOH906

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 504
ChainResidue
AALA350
ATHR353
AGLY354
ASER378
AGLY379
AHOH790

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO B 501
ChainResidue
AASN26
AARG43
BLEU29
BASP30
BSER31
BASP32
BHOH687
BHOH795

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO B 502
ChainResidue
BTRP326
BASN327
BGLY328
BGLY362
BALA367
BVAL370
BHOH823

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 503
ChainResidue
BSER319
BALA321
BGLU322
BLYS355
BHOH742
BHOH878

site_idAC8
Number of Residues9
Detailsbinding site for residue EDO B 504
ChainResidue
AHOH629
BGLY68
BARG69
BLEU78
BHOH601
BHOH658
BHOH794
BHOH871
BHOH888

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 505
ChainResidue
AHOH840
BLEU148
BHOH616
BHOH660
BHOH764

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO C 501
ChainResidue
CGLN96
CARG109
CGLY112
CLEU113
CHOH790

site_idAD2
Number of Residues8
Detailsbinding site for residue EDO C 502
ChainResidue
BARG261
BARG262
BASP265
CPRO74
CASP100
CVAL101
CHOH733
CHOH889

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO C 503
ChainResidue
CLYS166
CTYR171
CPRO400
CGLU403
CHOH837

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO C 504
ChainResidue
CALA296
CPRO298
CHOH672
CHOH764

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO C 505
ChainResidue
CLEU176
CPRO410
CTHR411
CHOH858

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO C 506
ChainResidue
CGLY18
CALA110
CLEU148
CVAL149
CHOH779

site_idAD7
Number of Residues8
Detailsbinding site for residue EDO D 501
ChainResidue
DVAL332
DHOH712
DHOH750
DGLY209
DSER210
DGLY233
DGLY234
DGLY331

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. GVLVRsDlNVP
ChainResidueDetails
AGLY18-PRO28

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00145","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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