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2CUN

Crystal structure of Phosphoglycerate Kinase from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
B0004618molecular_functionphosphoglycerate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
AARG114
AARG154
AGOL501
AHOH591

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 506
ChainResidue
BARG114
BARG154
BGOL502

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3PG A 503
ChainResidue
AGLY358
AGLY359
AHIS360
AGLY380
AGLY381
AGOL501
AHOH515
AHOH620
AARG34
ALYS200

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3PG B 504
ChainResidue
BARG34
BLYS200
BGLY358
BGLY359
BHIS360
BGLY380
BGLY381
BGOL502
BHOH509
BHOH551

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AASP19
AASN21
AARG34
AHIS57
AARG114
AALA150
A3PG503
ACL505

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BASP19
BASN21
BARG34
BHIS57
BALA150
BHIS153
BARG154
B3PG504
BCL506
BHOH575

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 507
ChainResidue
BALA33
BARG34
BGLY359
BILE362
BSER377
BTHR378

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 508
ChainResidue
AARG34
AGLY359
ASER377
ATHR378

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 509
ChainResidue
AASP89
AILE90
APHE91
AGLY92
AHOH542
BPHE115

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. TVFLRvDlNSP
ChainResidueDetails
ATHR13-PRO23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP19
BARG154
BGLU332
BGLY358
AHIS57
AARG114
AARG154
AGLU332
AGLY358
BASP19
BHIS57
BARG114

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
AARG34
BARG34

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
AARG34
AGLY359
AGLY381
ALYS200

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
BARG34
BGLY359
BGLY381
BLYS200

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PDB entries from 2024-07-17

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