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2O66

Crystal Structure of Arabidopsis thaliana PII bound to citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
C0006808biological_processregulation of nitrogen utilization
C0030234molecular_functionenzyme regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC A 201
ChainResidue
ALYS70
BARG115
BLYS125
BMET126
BTHR127
AILE98
AGLY99
AASP100
AGLY101
ALYS102
AHOH240
AHOH244
BARG113

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FLC B 202
ChainResidue
BLYS70
BILE98
BGLY99
BASP100
BGLY101
BLYS102
BHOH254
BHOH255
CARG113
CARG115
CLYS125

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC C 203
ChainResidue
AGLU64
AARG113
AARG115
CLYS70
CILE98
CGLY99
CASP100
CGLY101
CLYS102
CHOH216

Functional Information from PROSITE/UniProt
site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVlpV
ChainResidueDetails
ATHR95-VAL108

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY46
AGLY99
BGLY46
BGLY99
CGLY46
CGLY99

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17913711
ChainResidueDetails
AGLY48
BGLY48
CGLY48

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PDB entries from 2024-05-29

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