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1QMP

Phosphorylated aspartate in the crystal structure of the sporulation response regulator, Spo0A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000160biological_processphosphorelay signal transduction system
B0000160biological_processphosphorelay signal transduction system
C0000160biological_processphosphorelay signal transduction system
D0000160biological_processphosphorelay signal transduction system
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA W 301
ChainResidue
AASP10
APHD55
AILE57
AHOH404
AHOH413
BHOH425

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA X 301
ChainResidue
BHOH403
BHOH419
CHOH437
BASP10
BPHD55
BILE57

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA Y 301
ChainResidue
CASP10
CPHD55
CILE57
DHOH437
DHOH428
DHOH415

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA Z 301
ChainResidue
AHOH457
DASP10
DPHD55
DILE57
DHOH402
DHOH412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP9
DASP9
DASP10
DPHD55
AASP10
APHD55
BASP9
BASP10
BPHD55
CASP9
CASP10
CPHD55

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:10556024
ChainResidueDetails
APHD55
BPHD55
CPHD55
DPHD55

220113

PDB entries from 2024-05-22

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