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2GNK

GLNK, A SIGNAL PROTEIN FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
A0042802molecular_functionidentical protein binding
A0045848biological_processpositive regulation of nitrogen utilization
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 200
ChainResidue
AILE7
AALA64
AGLY87
AGLY89
ALYS90
AARG101
AARG103
AHOH203
AHOH232
AGLY27
ALEU28
ATHR29
AGLY35
AGLY37
ALYS58
AASP62
AVAL63

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

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgkiGDGKIFVaeL
ChainResidueDetails
ATHR83-LEU96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NUU
ChainResidueDetails
ATHR29

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9733647, ECO:0007744|PDB:2GNK
ChainResidueDetails
AGLY37
AALA64
AGLY87
AARG101

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17190799, ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NS1, ECO:0007744|PDB:2NUU
ChainResidueDetails
AARG38

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675
ChainResidueDetails
ATYR51

222415

PDB entries from 2024-07-10

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