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16PK

PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI BISUBSTRATE ANALOG

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0020015cellular_componentglycosome
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE BIS A 499
ChainResidue
AGLY217
APRO340
AGLY342
AVAL343
AGLU345
AGLY397
AGLY398
AGLY399
AHOH505
AHOH514
AHOH523
AALA218
AHOH571
AHOH673
AHOH766
AHOH768
AHOH779
AHOH781
AHOH799
AHOH872
AHOH874
AHOH902
ALYS223
AHOH981
AHOH1020
AHOH1032
AHOH1034
AHOH1037
AGLY241
AALA242
ATYR245
AALA314
ALEU315
AGLY339

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE EPE A 430
ChainResidue
ALYS49
ATHR52
AGLU53
AGLN251
AGLY252
ATYR253
AALA296
AGLU345
AMET346
AVAL347
APRO348
AHOH567
AHOH676
AHOH809
AHOH871

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. KVLIRvDfNVP
ChainResidueDetails
ALYS18-PRO28

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9000079, ECO:0007744|PDB:13PK
ChainResidueDetails
AASP24
AHIS62
ALYS223
AASN338
AGLU345
AGLY375

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9000079, ECO:0000269|PubMed:9642090, ECO:0007744|PDB:13PK
ChainResidueDetails
AARG39
AARG135
AARG172

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
AGLY376
AARG39
ALYS219
AGLY399

site_idMCSA1
Number of Residues4
DetailsM-CSA 40
ChainResidueDetails
AARG39electrostatic stabiliser, hydrogen bond donor
ALYS219electrostatic stabiliser, hydrogen bond donor
AGLY376electrostatic stabiliser, hydrogen bond donor
AGLY399electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-10

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