6DNH

Cryo-EM structure of human CPSF-160-WDR33-CPSF-30-PAS RNA complex at 3.4 A resolution

Replaces:  6BLL

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005847	cellular_component	mRNA cleavage and polyadenylation specificity factor complex
A	0006397	biological_process	mRNA processing
A	0019899	molecular_function	enzyme binding
A	0035925	molecular_function	mRNA 3'-UTR AU-rich region binding
A	0180012	biological_process	co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway
B	0031124	biological_process	mRNA 3'-end processing
C	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005847	cellular_component	mRNA cleavage and polyadenylation specificity factor complex
C	0006397	biological_process	mRNA processing
C	0008270	molecular_function	zinc ion binding
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0046872	molecular_function	metal ion binding
C	1990837	molecular_function	sequence-specific double-stranded DNA binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	CYS41
C	CYS49
C	CYS55
C	HIS59

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN C 302

Chain	Residue
C	CYS68
C	CYS76
C	CYS82
C	HIS86

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN C 303

Chain	Residue
C	CYS105
C	CYS110
C	HIS114
C	CYS96

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Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	13
Details	LIPOCALIN Lipocalin signature. EVKl.NLNGNWLLT

Chain	Residue	Details
B	GLU293-THR305

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	26
Details	ZN_FING: C3H1-type 1 => ECO:0000255|PROSITE-ProRule:PRU00723

Chain	Residue	Details
C	LYS35-SER61

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site_id	SWS_FT_FI2
Number of Residues	27
Details	ZN_FING: C3H1-type 2 => ECO:0000255|PROSITE-ProRule:PRU00723

Chain	Residue	Details
C	GLY62-ASP89

---

site_id	SWS_FT_FI3
Number of Residues	27
Details	ZN_FING: C3H1-type 3 => ECO:0000255|PROSITE-ProRule:PRU00723

Chain	Residue	Details
C	MET90-PRO117

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	ZN_FING: C3H1-type 4 => ECO:0000255|PROSITE-ProRule:PRU00723

Chain	Residue	Details
C	GLU118-HIS142
B	LYS560

---

site_id	SWS_FT_FI5
Number of Residues	26
Details	ZN_FING: C3H1-type 5 => ECO:0000255|PROSITE-ProRule:PRU00723

Chain	Residue	Details
C	THR143-PHE169

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	MET200

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332

Chain	Residue	Details
C	SER202

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	PRO212

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