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1QJM

Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution

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
A0006826biological_processiron ion transport
A0008236molecular_functionserine-type peptidase 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 SM A 690
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACO3692

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SM A 691
ChainResidue
AHIS595
ACO3693
AASP395
ATYR433
AARG463
ATYR526

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO3 A 692
ChainResidue
AASP60
ATYR92
AARG121
ASER122
AALA123
AGLY124
ASM690

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CO3 A 693
ChainResidue
AASP395
ATYR433
ATHR459
AARG463
ATHR464
AALA465
AALA466
ASM691

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101
ATYR433-SER442

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

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV
ChainResidueDetails
ALYS226-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 Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7
ChainResidueDetails
AASP60
ATYR92
ATYR192
AHIS253
AASP395
ATYR433
ATYR526
AHIS595

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475
ChainResidueDetails
ATHR117
AARG121
AALA123
AGLY124
ATHR459
AARG463
AALA465
AALA466

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.7
ChainResidueDetails
APRO430
AASN594
ATYR660

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN137
AASN281
AASN476

226707

PDB entries from 2024-10-30

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