eF-site ID 1xd3-ABCD PDB Code 1xd3 Chain A, B, C, D click to enlarge Title Crystal structure of UCHL3-UbVME complex Classification HYDROLASE Compound Ubiquitin Carboxyl-terminal esterase L3 Source Homo sapiens (Human) (UBIQ_HUMAN) Sequence A:  EGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPEL LSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVT SSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKK FLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPS IDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETL LEDAIEVCKKFMERDPDELRFNAIALSAA B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG C:  QRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLS MVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSS VYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFL EESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSID EKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLE DAIEVCKKFMERDPDELRFNAIALSAA D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG Description Functional site 1) chain C residue 163 type sequence D description BINDING SITE FOR RESIDUE MG C 2001 source : AC1 2) chain C residue 179 type sequence H description BINDING SITE FOR RESIDUE MG C 2003 source : AC3 3) chain C residue 78 type sequence Q description BINDING SITE FOR RESIDUE MG C 2005 source : AC5 4) chain C residue 79 type sequence D description BINDING SITE FOR RESIDUE MG C 2005 source : AC5 5) chain A residue 108 type sequence K description BINDING SITE FOR RESIDUE MG A 2006 source : AC6 6) chain A residue 109 type sequence D description BINDING SITE FOR RESIDUE MG A 2006 source : AC6 7) chain C residue 149 type sequence E description BINDING SITE FOR RESIDUE MG C 2007 source : AC7 8) chain C residue 79 type sequence D description BINDING SITE FOR RESIDUE MG C 2008 source : AC8 9) chain C residue 81 type sequence T description BINDING SITE FOR RESIDUE MG C 2008 source : AC8 10) chain C residue 181 type sequence Y description BINDING SITE FOR RESIDUE MG C 2008 source : AC8 11) chain A residue 21 type sequence K description BINDING SITE FOR RESIDUE MG A 2010 source : BC1 12) chain A residue 24 type sequence G description BINDING SITE FOR RESIDUE MG A 2010 source : BC1 13) chain A residue 25 type sequence L description BINDING SITE FOR RESIDUE MG A 2010 source : BC1 14) chain A residue 114 type sequence E description BINDING SITE FOR RESIDUE MG A 2010 source : BC1 15) chain A residue 58 type sequence I description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 16) chain A residue 89 type sequence Q description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 17) chain A residue 93 type sequence N description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 18) chain A residue 95 type sequence C description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 19) chain A residue 166 type sequence V description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 20) chain A residue 168 type sequence L description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 21) chain A residue 169 type sequence H description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 22) chain B residue 75 type sequence G description BINDING SITE FOR RESIDUE GVE B 1176 source : BC2 23) chain C residue 89 type sequence Q description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 24) chain C residue 93 type sequence N description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 25) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 26) chain C residue 166 type sequence V description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 27) chain C residue 168 type sequence L description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 28) chain C residue 169 type sequence H description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 29) chain D residue 75 type sequence G description BINDING SITE FOR RESIDUE GVE D 2276 source : BC3 30) chain A residue 89 type catalytic sequence Q description 597 source MCSA : MCSA1 31) chain A residue 95 type catalytic sequence C description 597 source MCSA : MCSA1 32) chain A residue 169 type catalytic sequence H description 597 source MCSA : MCSA1 33) chain A residue 184 type catalytic sequence D description 597 source MCSA : MCSA1 34) chain C residue 89 type catalytic sequence Q description 597 source MCSA : MCSA2 35) chain C residue 95 type catalytic sequence C description 597 source MCSA : MCSA2 36) chain C residue 169 type catalytic sequence H description 597 source MCSA : MCSA2 37) chain C residue 184 type catalytic sequence D description 597 source MCSA : MCSA2 38) chain A residue 95 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:19154770, ECO:0000269|PubMed:20380862, ECO:0000269|PubMed:9790970 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 95 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:19154770, ECO:0000269|PubMed:20380862, ECO:0000269|PubMed:9790970 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 169 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:P09936 source Swiss-Prot : SWS_FT_FI2 41) chain C residue 169 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:P09936 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 130 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 43) chain C residue 130 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 89-105 type prosite sequence QTISNACGTIGLIHAIA description UCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QtisNACGtigLIHAIA source prosite : PS00140 45) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 46) chain A residue 184 type SITE sequence D description Important for enzyme activity => ECO:0000250|UniProtKB:P09936 source Swiss-Prot : SWS_FT_FI3 47) chain C residue 184 type SITE sequence D description Important for enzyme activity => ECO:0000250|UniProtKB:P09936 source Swiss-Prot : SWS_FT_FI3

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