eF-site ID 4qq4-ABCD PDB Code 4qq4 Chain A, B, C, D click to enlarge Title CW-type zinc finger of MORC3 in complex with the amino terminus of histone H3 Classification METAL BINDING PROTEIN Compound MORC family CW-type zinc finger protein 3 Source Homo sapiens (Human) (H33_HUMAN) Sequence A:  PDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRN CEVPEEPE B:  PDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRN CEVPEEPE C:  ARTXQTARK D:  ARTXQTARK Description Functional site 1) chain A residue 436 type sequence S description BINDING SITE FOR RESIDUE CL A 2003 source : AC1 2) chain B residue 446 type sequence C description BINDING SITE FOR RESIDUE CL A 2003 source : AC1 3) chain A residue 446 type sequence C description BINDING SITE FOR RESIDUE CL A 2004 source : AC2 4) chain B residue 436 type sequence S description BINDING SITE FOR RESIDUE CL A 2004 source : AC2 5) chain A residue 406 type sequence P description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 6) chain A residue 407 type sequence D description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 7) chain A residue 408 type sequence Q description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 8) chain A residue 409 type sequence T description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 9) chain A residue 410 type sequence W description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 10) chain A residue 411 type sequence V description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 11) chain A residue 412 type sequence Q description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 12) chain A residue 419 type sequence W description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 13) chain A residue 424 type sequence D description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 14) chain A residue 430 type sequence P description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 15) chain A residue 431 type sequence E description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 16) chain A residue 453 type sequence E description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 17) chain B residue 407 type sequence D description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 18) chain B residue 431 type sequence E description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 19) chain D residue 4 type sequence X description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 20) chain D residue 5 type sequence Q description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 21) chain D residue 6 type sequence T description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 22) chain D residue 7 type sequence A description BINDING SITE FOR CHAIN C OF HISTONE H3.3 source : AC3 23) chain A residue 428 type sequence Q description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 24) chain A residue 429 type sequence L description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 25) chain A residue 430 type sequence P description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 26) chain A residue 431 type sequence E description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 27) chain B residue 406 type sequence P description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 28) chain B residue 407 type sequence D description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 29) chain B residue 408 type sequence Q description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 30) chain B residue 409 type sequence T description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 31) chain B residue 410 type sequence W description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 32) chain B residue 411 type sequence V description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 33) chain B residue 412 type sequence Q description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 34) chain B residue 419 type sequence W description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 35) chain B residue 424 type sequence D description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 36) chain B residue 430 type sequence P description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 37) chain B residue 431 type sequence E description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 38) chain C residue 1 type sequence A description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 39) chain C residue 2 type sequence R description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 40) chain C residue 3 type sequence T description BINDING SITE FOR CHAIN D OF HISTONE H3.3 source : AC4 41) chain C residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI5 42) chain D residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 2 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 2 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 3 type MOD_RES sequence T description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 46) chain D residue 3 type MOD_RES sequence T description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 435 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 446 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 413 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 416 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 435 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 446 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 4 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 54) chain D residue 4 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 55) chain C residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI4 56) chain D residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI4 57) chain C residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P84244 source Swiss-Prot : SWS_FT_FI6 58) chain D residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P84244 source Swiss-Prot : SWS_FT_FI6 59) chain C residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7309716 source Swiss-Prot : SWS_FT_FI7 60) chain D residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7309716 source Swiss-Prot : SWS_FT_FI7

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