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3TTR

Crystal structure of C-lobe of bovine lactoferrin complexed with Lidocaine at 2.27 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlAVAVVKKA
ChainResidueDetails
ATYR433-ALA442

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLaedvGDVAF
ChainResidueDetails
ATYR526-PHE542

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DFrLLClDgtrkp...VteaqsChlAvapnHaVV
ChainResidueDetails
AASP568-VAL598

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF
ChainResidueDetails
AASP395
ATYR433
ATYR526
AHIS595

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
ChainResidueDetails
ATHR459
AARG463
AALA465
AGLY466

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF
ChainResidueDetails
AASN368
AASN476

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF
ChainResidueDetails
AASN545

227561

PDB entries from 2024-11-20

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