5E6S

Structures of leukocyte integrin aLB2: The aI domain, the headpiece, and the pocket for the internal ligand

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0007155	biological_process	cell adhesion
A	0008305	cellular_component	integrin complex
C	0007155	biological_process	cell adhesion
C	0008305	cellular_component	integrin complex
E	0007155	biological_process	cell adhesion
E	0008305	cellular_component	integrin complex

Functional Information from PROSITE/UniProt

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CrCdtGyiGKnC

Chain	Residue	Details
B	CYS448-CYS459

---

site_id	PS01186
Number of Residues	12
Details	EGF_2 EGF-like domain signature 2. CrCdtGYigkn....C

Chain	Residue	Details
B	CYS448-CYS459

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN

Chain	Residue	Details
B	SER114
A	ASP569
A	ASP573
C	ASP443
C	ASP445
C	ASP447
C	GLU451
C	ASP505
C	ASN507
C	ASP509
C	ASP513
B	SER116
C	ASP565
C	ASP569
C	ASP573
E	ASP443
E	ASP445
E	ASP447
E	GLU451
E	ASP505
E	ASN507
E	ASP509
B	GLU212
E	ASP513
E	ASP565
E	ASP569
E	ASP573
D	SER114
D	SER116
D	GLU212
F	SER114
F	SER116
F	GLU212

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72

Chain	Residue	Details
B	ASP119
C	ARG645
C	ARG701
C	ASN705
E	ASN40
E	ASN64
E	ASN624
E	ARG645
E	ARG701
E	ASN705
D	ASP119
F	ASP119
A	ARG645
A	ARG701
A	ASN705
C	ASN40
C	ASN64
C	ASN624

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN

Chain	Residue	Details
B	ASP120
D	ASP120
F	ASP120

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN

Chain	Residue	Details
B	ASP151
F	ASN207
F	ASP209
F	PRO211
B	ASN207
B	ASP209
B	PRO211
D	ASP151
D	ASN207
D	ASP209
D	PRO211
F	ASP151

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN

Chain	Residue	Details
B	ASP242
D	ASP242
F	ASP242

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH

Chain	Residue	Details
B	GLU325
D	GLU325
F	GLU325

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816

Chain	Residue	Details
B	GLN1
D	GLN1
F	GLN1

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973

Chain	Residue	Details
B	ASN28
D	ASN28
F	ASN28

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN

Chain	Residue	Details
B	ASN94
D	ASN94
F	ASN94

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973

Chain	Residue	Details
B	ASN190
D	ASN190
F	ASN190

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
B	LYS232
D	LYS232
F	LYS232

---