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1BIY

STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0001503biological_processossification
A0001817biological_processregulation of cytokine production
A0002227biological_processinnate immune response in mucosa
A0002376biological_processimmune system process
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0019732biological_processantifungal humoral response
A0031665biological_processnegative regulation of lipopolysaccharide-mediated signaling pathway
A0032680biological_processregulation of tumor necrosis factor production
A0033690biological_processpositive regulation of osteoblast proliferation
A0042581cellular_componentspecific granule
A0043066biological_processnegative regulation of apoptotic process
A0045669biological_processpositive regulation of osteoblast differentiation
A0046872molecular_functionmetal ion binding
A0055037cellular_componentrecycling endosome
A0060349biological_processbone morphogenesis
A1900159biological_processpositive regulation of bone mineralization involved in bone maturation
A1900229biological_processnegative regulation of single-species biofilm formation in or on host organism
A1902732biological_processpositive regulation of chondrocyte proliferation
A2000308biological_processnegative regulation of tumor necrosis factor (ligand) superfamily member 11 production
A2001205biological_processnegative regulation of osteoclast development
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 690
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACO3692

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 691
ChainResidue
AASP395
ATYR433
ATYR526
AHIS595
ACO3693

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 A 692
ChainResidue
AASP60
ATYR92
ATHR117
AARG121
AALA123
AGLY124
ATYR192
AHIS253
AFE690

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CO3 A 693
ChainResidue
AASP395
ATYR433
ATHR459
AARG463
ATHR464
AALA465
AGLY466
ATYR526
AHIS595
AFE691

site_idFE1
Number of Residues5
DetailsIRON BINDING SITE IN N-LOBE.
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACO3692

site_idFE2
Number of Residues5
DetailsIRON BINDING SITE IN C-LOBE.
ChainResidue
ACO3693
AASP395
ATYR433
ATYR526
AHIS595

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101
ATYR433-ALA442

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF
ChainResidueDetails
ATYR192-PHE208
ATYR526-PHE542

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNntrap...VdafkeChlAqvpsHaVV
ChainResidueDetails
AGLN226-VAL256
AASP568-VAL598

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741
ChainResidueDetails
ALYS73

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741
ChainResidueDetails
ASER259

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
ChainResidueDetails
AASP60
ATYR92
AHIS253
AASP395
ATYR433
ATYR526
AHIS595

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
ChainResidueDetails
ATHR117
AARG121
AALA123
AGLY124
ATHR459
AARG463
AALA465
AGLY466

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
ChainResidueDetails
ATYR192

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
ChainResidueDetails
AASN233
AASN545

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
ChainResidueDetails
AASN281

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
ChainResidueDetails
AASN476

218853

PDB entries from 2024-04-24

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