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

7JRD

The crystal structure of lactoferrin binding protein B (LbpB) from Neisseria meningitidis in complex with human lactoferrin

Functional Information from GO Data
ChainGOidnamespacecontents
B0001503biological_processossification
B0001530molecular_functionlipopolysaccharide binding
B0001817biological_processregulation of cytokine production
B0002227biological_processinnate immune response in mucosa
B0002376biological_processimmune system process
B0003677molecular_functionDNA binding
B0004252molecular_functionserine-type endopeptidase activity
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005769cellular_componentearly endosome
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0006826biological_processiron ion transport
B0006959biological_processhumoral immune response
B0008201molecular_functionheparin binding
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0009986cellular_componentcell surface
B0019731biological_processantibacterial humoral response
B0019732biological_processantifungal humoral response
B0030141cellular_componentsecretory granule
B0031640biological_processkilling of cells of another organism
B0031665biological_processnegative regulation of lipopolysaccharide-mediated signaling pathway
B0032680biological_processregulation of tumor necrosis factor production
B0032780biological_processnegative regulation of ATP-dependent activity
B0032991cellular_componentprotein-containing complex
B0033690biological_processpositive regulation of osteoblast proliferation
B0034145biological_processpositive regulation of toll-like receptor 4 signaling pathway
B0035580cellular_componentspecific granule lumen
B0042581cellular_componentspecific granule
B0042742biological_processdefense response to bacterium
B0043066biological_processnegative regulation of apoptotic process
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044793biological_processnegative regulation by host of viral process
B0045071biological_processnegative regulation of viral genome replication
B0045669biological_processpositive regulation of osteoblast differentiation
B0046872molecular_functionmetal ion binding
B0048525biological_processnegative regulation of viral process
B0050829biological_processdefense response to Gram-negative bacterium
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0055037cellular_componentrecycling endosome
B0060349biological_processbone morphogenesis
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0070062cellular_componentextracellular exosome
B0071902biological_processpositive regulation of protein serine/threonine kinase activity
B0097013cellular_componentphagocytic vesicle lumen
B0140912molecular_functionmembrane destabilizing activity
B1900159biological_processpositive regulation of bone mineralization involved in bone maturation
B1900229biological_processnegative regulation of single-species biofilm formation in or on host organism
B1902732biological_processpositive regulation of chondrocyte proliferation
B1904724cellular_componenttertiary granule lumen
B2000117biological_processnegative regulation of cysteine-type endopeptidase activity
B2000308biological_processnegative regulation of tumor necrosis factor (ligand) superfamily member 11 production
B2001205biological_processnegative regulation of osteoclast development
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
BTYR93-GLY102
BTYR436-SER445

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
ChainResidueDetails
BTYR193-PHE209
BTYR529-PHE545

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
ChainResidueDetails
BGLU227-VAL257
BASP571-VAL601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064
ChainResidueDetails
BLYS74

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064
ChainResidueDetails
BSER260

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
ChainResidueDetails
BASP61
BTYR93
BTYR193
BHIS254
BASP396
BTYR436
BTYR529
BHIS598

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
ChainResidueDetails
BTHR118
BARG122
BALA124
BGLY125
BTHR462
BARG466
BALA468
BGLY469

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interaction with PspA
ChainResidueDetails
BARG5
BGLN14

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for iron binding
ChainResidueDetails
BARG211

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8069634, ECO:0000269|Ref.72
ChainResidueDetails
BASN138

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.72
ChainResidueDetails
BASN479

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
ChainResidueDetails
BASN624

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon