Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1X89

Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S

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 Residues11
DetailsBINDING SITE FOR RESIDUE CM1 A 200
ChainResidue
ATYR52
ALYS134
ATYR138
ATHR54
ASER68
ALEU70
AARG72
ATRP79
AARG81
APHE123
ALYS125

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CM1 B 200
ChainResidue
BTYR52
BTHR54
BSER68
BLEU70
BTRP79
BARG81
BPHE123
BLYS125
BLYS134
BTYR138

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CM1 C 200
ChainResidue
CTYR52
CTHR54
CSER68
CLEU70
CARG72
CTRP79
CARG81
CPHE123
CLYS125
CPHE133
CLYS134
CTYR138

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon