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1YLH

Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004612molecular_functionphosphoenolpyruvate carboxykinase (ATP) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 560
ChainResidue
ALYS213
AHIS232
AASP269
AHOH753
AHOH863
AHOH864

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 921
ChainResidue
ATHR252
AGLY253
ALYS254
ATHR255
AHOH818
ALEU249
ASER250
AGLY251

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 922
ChainResidue
AARG154
ATYR339
AARG346
AHOH656

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DT3 A 592
ChainResidue
ALEU108
ALYS111
AGLN112
ACYS175
ATHR176

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 593
ChainResidue
ACYS74
ALYS79
ATRP84

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 594
ChainResidue
ALEU265
AASP268
ACYS285
ATYR336
AHOH872

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 931
ChainResidue
AARG65
ATYR207
ALYS213
AARG333
APHE413
AHOH753
AHOH857
AHOH864

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 900
ChainResidue
AALA56
AASP58
ALYS328
AHOH657
AHOH694

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 901
ChainResidue
APHE44
AASP58
AGLY60
ATHR63
AASN312

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 902
ChainResidue
APHE44
AGLY60
AILE61
AGLY204
ATRP206
AHOH613

Functional Information from PROSITE/UniProt
site_idPS00532
Number of Residues16
DetailsPEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdEsGVfN
ChainResidueDetails
ALEU265-ASN280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AARG65
AARG154
ATYR207
AGLY248
AARG333
AARG346

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453
ChainResidueDetails
ALYS213
AGLU297
AARG449
ATHR455

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:15983413
ChainResidueDetails
AHIS232
AASP269

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
ALYS254
AARG333
AHIS232

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AARG333
AHIS232

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PDB entries from 2024-07-24

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