eF-site ID 3tzs-B PDB Code 3tzs Chain B click to enlarge Title Crystal structure of Neutrophil gelatinase-associated lipocalin NGAL (C87S mutant) in complex with fragment 1026, phenylurea Classification APOPTOSIS Compound Neutrophil gelatinase-associated lipocalin Source (NGAL_HUMAN) Sequence B:  SDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILRE DKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFV PGSQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFK KVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPEN HIVFPVPIDQCID Description Functional site 1) chain B residue 25 type sequence N description BINDING SITE FOR RESIDUE PHU A 185 source : AC5 2) chain B residue 26 type sequence Q description BINDING SITE FOR RESIDUE PHU A 185 source : AC5 3) chain B residue 86 type sequence G description BINDING SITE FOR RESIDUE EDO A 186 source : AC6 4) chain B residue 41 type sequence I description BINDING SITE FOR RESIDUE PHU B 201 source : AC7 5) chain B residue 123 type sequence F description BINDING SITE FOR RESIDUE PHU B 201 source : AC7 6) chain B residue 132 type sequence Y description BINDING SITE FOR RESIDUE PHU B 201 source : AC7 7) chain B residue 134 type sequence K description BINDING SITE FOR RESIDUE PHU B 201 source : AC7 8) chain B residue 8 type sequence I description BINDING SITE FOR RESIDUE SO4 B 206 source : AC8 9) chain B residue 75 type sequence K description BINDING SITE FOR RESIDUE SO4 B 206 source : AC8 10) chain B residue 164 type sequence N description BINDING SITE FOR RESIDUE SO4 B 206 source : AC8 11) chain B residue 165 type sequence H description BINDING SITE FOR RESIDUE SO4 B 206 source : AC8 12) chain B residue 52 type sequence Y description BINDING SITE FOR RESIDUE CL B 183 source : AC9 13) chain B residue 54 type sequence T description BINDING SITE FOR RESIDUE CL B 183 source : AC9 14) chain B residue 134 type sequence K description BINDING SITE FOR RESIDUE CL B 183 source : AC9 15) chain B residue 138 type sequence Y description BINDING SITE FOR RESIDUE CL B 183 source : AC9 16) chain B residue 81 type sequence R description BINDING SITE FOR RESIDUE SO4 B 184 source : BC1 17) chain B residue 106 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 184 source : BC1 18) chain B residue 134 type sequence K description BINDING SITE FOR RESIDUE SO4 B 184 source : BC1 19) chain B residue 23 type sequence Q description BINDING SITE FOR RESIDUE PHU C 186 source : BC7 20) chain B residue 26 type sequence Q description BINDING SITE FOR RESIDUE PHU C 186 source : BC7 21) chain B residue 25 type sequence N description BINDING SITE FOR RESIDUE SO4 C 188 source : BC9 22) chain B residue 52 type BINDING sequence Y description BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U source Swiss-Prot : SWS_FT_FI1 23) chain B residue 106 type BINDING sequence Y description BINDING => ECO:0007744|PDB:3CMP source Swiss-Prot : SWS_FT_FI2 24) chain B residue 134 type BINDING sequence K description BINDING => ECO:0007744|PDB:3CMP source Swiss-Prot : SWS_FT_FI2 25) chain B residue 125 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U source Swiss-Prot : SWS_FT_FI3 26) chain B residue 138 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U source Swiss-Prot : SWS_FT_FI3 27) chain B residue 65 type CARBOHYD sequence N description 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 source Swiss-Prot : SWS_FT_FI5

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