5NVN

Crystal structure of the human 4EHP-4E-BP1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003743	molecular_function	translation initiation factor activity
A	0005737	cellular_component	cytoplasm
A	0006413	biological_process	translational initiation
B	0008190	molecular_function	eukaryotic initiation factor 4E binding
B	0045947	biological_process	negative regulation of translational initiation
C	0003723	molecular_function	RNA binding
C	0003743	molecular_function	translation initiation factor activity
C	0005737	cellular_component	cytoplasm
C	0006413	biological_process	translational initiation
D	0008190	molecular_function	eukaryotic initiation factor 4E binding
D	0045947	biological_process	negative regulation of translational initiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue FMT A 301

Chain	Residue
A	GLN93
A	ARG96
A	HOH439
B	PRO72
B	ASP74
C	ASP198

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site_id	AC2
Number of Residues	3
Details	binding site for residue FMT C 301

Chain	Residue
B	ARG73
C	THR199
C	ARG202

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site_id	AC3
Number of Residues	5
Details	binding site for residue FMT C 302

Chain	Residue
B	ARG73
C	PHE160
C	MET161
C	ARG195
C	THR199

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site_id	AC4
Number of Residues	4
Details	binding site for residue FMT C 303

Chain	Residue
C	LEU139
C	ARG140
C	LEU143
C	FMT304

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site_id	AC5
Number of Residues	2
Details	binding site for residue FMT C 304

Chain	Residue
C	GLU177
C	FMT303

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site_id	AC6
Number of Residues	5
Details	binding site for residue FMT C 305

Chain	Residue
C	ARG146
C	ASN150
C	ASN205
C	HOH416
D	ARG56

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site_id	AC7
Number of Residues	1
Details	binding site for residue FMT C 306

Chain	Residue
C	LYS222

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Functional Information from PROSITE/UniProt

site_id	PS00813
Number of Residues	24
Details	IF4E Eukaryotic initiation factor 4E signature. DFhlFKegIkPmWEDdanknGGKW

Chain	Residue	Details
A	ASP112-TRP135

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648

Chain	Residue	Details
B	THR50
D	THR50
C	TYR78
C	LYS222

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
B	TYR54
D	TYR54
A	ARG174
C	HIS110
C	TRP124
C	ARG174

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR => ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	SER65
D	SER65

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by MTOR => ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	THR70
D	THR70

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	THR77
D	THR77
C	LYS222

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
B	SER83
D	SER83

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site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:22578813

Chain	Residue	Details
B	LYS57
D	LYS57

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