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3FW4

Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Ferric Catechol

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 Residues2
DetailsBINDING SITE FOR RESIDUE FE A 179
ChainResidue
ATYR106
ACAQ180

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAQ A 180
ChainResidue
ATYR106
APHE123
ALYS125
ATYR132
ALYS134
AFE179

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 183
ChainResidue
AARG81
ATYR138
ATHR54

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 184
ChainResidue
ALYS142
AGLU143
AASP173
CGLN20

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 185
ChainResidue
AASN96
ASER99

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 186
ChainResidue
ATHR145
ASER146
AGLU147

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 188
ChainResidue
ALYS125

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 190
ChainResidue
AHIS118

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FE B 179
ChainResidue
BARG81

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 180
ChainResidue
BTYR52

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 181
ChainResidue
BTRP79
BARG81
BTYR100

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FE C 179
ChainResidue
CCAQ180

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAQ C 180
ChainResidue
CPHE123
CLYS125
CLYS134
CFE179
CGOL188

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA C 181
ChainResidue
AGLN117
CHOH272

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA C 182
ChainResidue
ALYS75

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA C 183
ChainResidue
CSER146

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA C 184
ChainResidue
CHOH266

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 185
ChainResidue
CTRP79
CARG81

site_idCC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL C 186
ChainResidue
CPHE22
CASP24
CPRO85
CGLN88
CPRO89
CGLY90
CGLU91
CPHE92
CHOH211
CHOH300
CHOH320

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 187
ChainResidue
CPRO85
CLEU94
CILE97
CTYR106
CHOH326

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 188
ChainResidue
CALA40
CLYS125
CTYR132
CCAQ180
CHOH297

site_idCC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 189
ChainResidue
CLEU18
CGLN19
CGLN20
CVAL111
CSER112
CHOH239
CHOH259

site_idCC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL C 190
ChainResidue
CARG130

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 3731
ChainResidue
CLYS59
CGLU60
CASP61

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 191
ChainResidue
BGLN23
CASN116
CARG140
CHOH279

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQdnQFQGKWYVV
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
ATYR52
BTYR52
CTYR52

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:3CMP
ChainResidueDetails
ATYR106
ALYS134
BTYR106
BLYS134
CTYR106
CLYS134

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
ALYS125
ATYR138
BLYS125
BTYR138
CLYS125
CTYR138

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

225158

PDB entries from 2024-09-18

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