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5JR8

Disposal of Iron by a Mutant form of Siderocalin NGAL

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 Residues7
Detailsbinding site for residue PO4 A 201
ChainResidue
AARG81
ATYR106
ALYS125
ALYS134
AHOH302
AHOH314
AHOH322

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 B 201
ChainResidue
BSER68
BARG81
BLYS134
BTYR138
BPO4203
BTYR52
BTHR54

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL B 202
ChainResidue
AILE55
AGLU57
ATYR78
BLEU18
BGLN19
BGLN20
BVAL111
BSER112

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 B 203
ChainResidue
BTRP79
BARG81
BTYR106
BLYS125
BLYS134
BPO4201
BHOH305

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 Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
ATYR52
BTYR52

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:3CMP
ChainResidueDetails
ATYR106
ALYS134
BTYR106
BLYS134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U
ChainResidueDetails
BLYS125
BTYR138
ALYS125
ATYR138

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

221051

PDB entries from 2024-06-12

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