4RR2

Crystal structure of human primase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000428	cellular_component	DNA-directed RNA polymerase complex
A	0003896	molecular_function	DNA primase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005658	cellular_component	alpha DNA polymerase:primase complex
A	0006260	biological_process	DNA replication
A	0006269	biological_process	DNA replication, synthesis of primer
A	0006270	biological_process	DNA replication initiation
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0016779	molecular_function	nucleotidyltransferase activity
A	0032553	molecular_function	ribonucleotide binding
A	0046872	molecular_function	metal ion binding
A	1990077	cellular_component	primosome complex
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005658	cellular_component	alpha DNA polymerase:primase complex
B	0006260	biological_process	DNA replication
B	0006261	biological_process	DNA-templated DNA replication
B	0006269	biological_process	DNA replication, synthesis of primer
B	0006270	biological_process	DNA replication initiation
B	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0071667	molecular_function	DNA/RNA hybrid binding
B	1903934	biological_process	positive regulation of DNA primase activity
B	1990077	cellular_component	primosome complex
C	0000287	molecular_function	magnesium ion binding
C	0000428	cellular_component	DNA-directed RNA polymerase complex
C	0003896	molecular_function	DNA primase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005658	cellular_component	alpha DNA polymerase:primase complex
C	0006260	biological_process	DNA replication
C	0006269	biological_process	DNA replication, synthesis of primer
C	0006270	biological_process	DNA replication initiation
C	0008270	molecular_function	zinc ion binding
C	0016020	cellular_component	membrane
C	0016779	molecular_function	nucleotidyltransferase activity
C	0032553	molecular_function	ribonucleotide binding
C	0046872	molecular_function	metal ion binding
C	1990077	cellular_component	primosome complex
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005658	cellular_component	alpha DNA polymerase:primase complex
D	0006260	biological_process	DNA replication
D	0006261	biological_process	DNA-templated DNA replication
D	0006269	biological_process	DNA replication, synthesis of primer
D	0006270	biological_process	DNA replication initiation
D	0046872	molecular_function	metal ion binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0071667	molecular_function	DNA/RNA hybrid binding
D	1903934	biological_process	positive regulation of DNA primase activity
D	1990077	cellular_component	primosome complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 800

Chain	Residue
A	CYS121
A	CYS122
A	CYS128
A	CYS131

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 900

Chain	Residue
C	CYS121
C	CYS122
C	CYS128
C	CYS131

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 D 1000

Chain	Residue
D	CYS287
D	CYS367
D	CYS384
D	CYS424
D	LEU441
D	PRO444
D	PRO285

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377

Chain	Residue	Details
B	CYS287
B	CYS367
B	CYS424
D	CYS287
D	CYS367
D	CYS424

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159

Chain	Residue	Details
B	CYS384
D	CYS384
A	ASP306
C	ASP109
C	ASP111
C	ASP306

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	THR470
D	THR470
A	CYS128
A	CYS131
C	CYS121
C	CYS122
C	CYS128
C	CYS131

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:31479243

Chain	Residue	Details
A	SER160
C	SER160

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:31479243

Chain	Residue	Details
A	HIS315
C	HIS315

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:31479243

Chain	Residue	Details
A	HIS324
C	HIS324

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895

Chain	Residue	Details
A	MET1
C	MET1

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