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4IAW

Engineered human lipocalin 2 (C26) 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
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006826biological_processiron ion transport
C0006915biological_processapoptotic process
C0015891biological_processsiderophore transport
C0031410cellular_componentcytoplasmic vesicle
C0035580cellular_componentspecific granule lumen
C0036094molecular_functionsmall molecule binding
C0042742biological_processdefense response to bacterium
C0042802molecular_functionidentical protein binding
C0045087biological_processinnate immune response
C0060205cellular_componentcytoplasmic vesicle lumen
C0070062cellular_componentextracellular exosome
C0120162biological_processpositive regulation of cold-induced thermogenesis
C0140315molecular_functioniron ion sequestering activity
C1903981molecular_functionenterobactin binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE LIZ A 201
ChainResidue
AGLN33
APHE123
ASER136
AYT3202
AHOH312
AHOH334
AHOH347
AHOH377
AHOH381
AHOH383
AHOH386
AARG36
BTHR4
ATHR52
AGLN54
AVAL66
AALA68
AARG70
AMET81
ATYR106

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE YT3 A 202
ChainResidue
ALIZ201
AHOH377

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LIZ B 201
ChainResidue
ATHR4
BGLN33
BARG36
BTHR52
BGLN54
BVAL66
BALA68
BARG70
BLEU79
BMET81
BTYR106
BPHE123
BSER136
BYT3202
BHOH314
BHOH315
BHOH327
BHOH341

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE YT3 B 202
ChainResidue
BLIZ201
BHOH341

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LIZ C 201
ChainResidue
CGLN33
CTHR52
CGLN54
CVAL66
CALA68
CARG70
CGLU77
CLEU79
CPHE83
CTYR106
CPHE123
CSER136
CYT3202

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE YT3 C 202
ChainResidue
CLIZ201

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 Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
ATHR52
BTHR52
CTHR52

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:3CMP
ChainResidueDetails
ATYR106
ASER134
BTYR106
BSER134
CTYR106
CSER134

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
BLEU138
CLYS125
CLEU138
ALYS125
ALEU138
BLYS125

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678
ChainResidueDetails
AGLN1
BGLN1
CGLN1

site_idSWS_FT_FI5
Number of Residues3
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
CASN65

221051

PDB entries from 2024-06-12

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