Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1L6M

Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition

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 Residues3
DetailsBINDING SITE FOR RESIDUE FE A 200
ChainResidue
ADBH201
ADBH202
ADBS203

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE B 300
ChainResidue
BDBH301
BDBH302
BDBS303

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FE C 400
ChainResidue
CDBH401
CDBS403

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 230
ChainResidue
AASP61
ASER63
ATHR82
ALYS59

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 330
ChainResidue
CLYS59
CASP61
CSER63
CTHR82

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 430
ChainResidue
ALYS75
CASN164
CHIS165

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DBH A 201
ChainResidue
ATYR52
ASER68
ATRP79
AARG81
ALYS134
AFE200
ADBH202
ADBS203

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DBH A 202
ChainResidue
ATRP79
AARG81
ALEU94
ATYR100
ATYR106
ALYS125
AFE200
ADBH201
ADBS203

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DBS A 203
ChainResidue
AALA40
ATYR106
APHE123
ALYS125
ATYR132
ALYS134
AFE200
ADBH201
ADBH202
AHOH501

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DBH B 301
ChainResidue
BSER68
BARG81
BLYS134
BFE300
BDBH302
BDBS303
BHOH509

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DBH B 302
ChainResidue
BTYR106
BLYS125
BFE300
BDBH301
BDBS303

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DBS B 303
ChainResidue
BALA40
BTYR106
BPHE123
BLYS125
BLYS134
BFE300
BDBH301
BDBH302

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DBH C 401
ChainResidue
CTYR52
CSER68
CTRP79
CARG81
CPHE123
CLYS134
CFE400
CDBS403

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DBS C 403
ChainResidue
CALA40
CTYR106
CPHE123
CLYS125
CLYS134
CFE400
CDBH401

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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon