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4AFF

High resolution structure of a PII mutant (I86N) protein in complex with ATP, MG and FLC

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006351biological_processDNA-templated transcription
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP A 1117
ChainResidue
AILE7
AVAL64
AASN86
AGLY87
AASP88
AGLY89
ALYS90
AARG101
AARG103
AMG1118
AFLC1119
AGLY27
AHOH2061
AHOH2104
AHOH2114
AHOH2130
AMET28
ATHR29
AGLY35
APHE36
AGLY37
AARG38
AGLU62

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1118
ChainResidue
AATP1117
AFLC1119

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FLC A 1119
ChainResidue
APHE36
AGLY37
AARG38
AGLN39
ALYS40
ALEU56
AASN86
AGLY87
AASN108
AATP1117
AMG1118
AHOH2061
AHOH2062
AHOH2065
AHOH2073
AHOH2102
AHOH2121

Functional Information from PROSITE/UniProt
site_idPS00496
Number of Residues6
DetailsPII_GLNB_UMP P-II protein uridylation site. YRGSEY
ChainResidueDetails
ATYR46-TYR51

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgenGDGKIFVspV
ChainResidueDetails
ATHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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