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2NS1

Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008519molecular_functionammonium channel activity
A0015670biological_processcarbon dioxide transport
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0072488biological_processammonium transmembrane transport
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
B0042802molecular_functionidentical protein binding
B0045848biological_processpositive regulation of nitrogen utilization
Functional Information from PROSITE/UniProt
site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgkiGDGKIFVaeL
ChainResidueDetails
BTHR83-LEU96

site_idPS01219
Number of Residues26
DetailsAMMONIUM_TRANSP Ammonium transporters signature. DFAGGtvVhinAAiaGLvgaYLiGkR
ChainResidueDetails
AASP160-ARG185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NUU
ChainResidueDetails
BTHR29
AGLY69-GLN97
AGLY150-GLY163
AALA220-ILE226
AILE279-GLY280
AALA334-MET348

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9733647, ECO:0007744|PDB:2GNK
ChainResidueDetails
BGLY37
ACYS312-ALA333
AGLY349-ALA377
BALA64
BGLY87
BARG101
AGLY164-ALA179
AMET200-SER219
AALA227-ALA251
ALEU258-TYR278
AVAL281-VAL299

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
BARG38
AGLU121-ARG124
ATYR180-PRO199
ALEU252-SER257
ATHR300-PRO311

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675
ChainResidueDetails
BPHE51

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15361618
ChainResidueDetails
ASER219

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for the deprotonation of the ammonium cation => ECO:0000269|PubMed:19278252
ChainResidueDetails
AASP160

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Twin-His motif. Important for optimum substrate conductance => ECO:0000305|PubMed:17040913, ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768
ChainResidueDetails
AHIS168
AHIS318

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Important for optimum substrate conductance => ECO:0000305|PubMed:18362341
ChainResidueDetails
APHE215

223166

PDB entries from 2024-07-31

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