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3DSZ

Engineered human lipocalin 2 in complex with Y-DTPA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006826biological_processiron ion transport
A0006915biological_processapoptotic process
A0015891biological_processsiderophore transport
A0031410cellular_componentcytoplasmic vesicle
A0035580cellular_componentspecific granule lumen
A0036094molecular_functionsmall molecule binding
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0045087biological_processinnate immune response
A0060205cellular_componentcytoplasmic vesicle lumen
A0070062cellular_componentextracellular exosome
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0140315molecular_functioniron ion sequestering activity
A1903981molecular_functionenterobactin binding
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006826biological_processiron ion transport
B0006915biological_processapoptotic process
B0015891biological_processsiderophore transport
B0031410cellular_componentcytoplasmic vesicle
B0035580cellular_componentspecific granule lumen
B0036094molecular_functionsmall molecule binding
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0045087biological_processinnate immune response
B0060205cellular_componentcytoplasmic vesicle lumen
B0070062cellular_componentextracellular exosome
B0120162biological_processpositive regulation of cold-induced thermogenesis
B0140315molecular_functioniron ion sequestering activity
B1903981molecular_functionenterobactin binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE LIZ A 187
ChainResidue
AGLN33
ATYR106
APHE123
ATHR136
AHOH189
AHOH193
AHOH197
AHOH219
AHOH323
AHOH334
AHOH345
AARG36
ATHR52
AGLN54
AALA68
AARG70
AASP77
ATYR78
ALEU79

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LIZ B 187
ChainResidue
AHOH189

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE YT3 B 188
ChainResidue
ALYS73
ALYS74
BGLN33
BARG36
BTHR52
BGLN54
BALA68
BARG70
BASP77
BLEU79
BTYR106
BPHE123
BTHR136
BHOH223
BHOH231
BHOH237
BHOH263
BHOH280
BHOH296

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE YT3 A 188
ChainResidue
BHOH223

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQdnQFHGKWYQV
ChainResidueDetails
AASN21-VAL34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
BTHR52
ATHR52

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:3CMP
ChainResidueDetails
ATYR106
ASER134
BTYR106
BSER134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
BLYS125
BLEU138
ALYS125
ALEU138

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678
ChainResidueDetails
AGLN1
BGLN1

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10684642, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7683678, ECO:0007744|PDB:1DFV, ECO:0007744|PDB:1QQS
ChainResidueDetails
AASN65
BASN65

220472

PDB entries from 2024-05-29

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