4XH2

Crystal structure of human paxillin LD4 motif in complex with Fab fragment

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue GOL B 301

Chain	Residue
B	THR5
B	GLN6
B	PHE98
B	GLN100
B	HOH434

---

site_id	AC2
Number of Residues	7
Details	binding site for residue GOL B 302

Chain	Residue
B	ASP167
B	HOH432
B	HOH448
A	HIS164
B	THR164
B	GLU165
B	GLN166

---

site_id	AC3
Number of Residues	9
Details	binding site for residue GOL C 301

Chain	Residue
C	SER130
C	HOH423
C	HOH445
D	SER114
D	PHE116
D	LYS207
E	GLY134
E	THR135
E	PRO185

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL C 302

Chain	Residue
C	GLY134
C	THR135
C	HOH402
C	HOH428
C	HOH450
F	SER114
F	ASN138
F	HOH420
F	HOH482

---

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL D 301

Chain	Residue
C	LYS214
D	TYR186
D	ASN210
D	ARG211
D	GLY212
D	GLU213

---

site_id	AC6
Number of Residues	11
Details	binding site for residue PO4 D 302

Chain	Residue
C	LYS129
C	HOH430
D	THR206
D	LYS207
D	HOH402
D	HOH408
D	HOH431
D	HOH433
D	HOH456
E	GLY133
E	HOH326

---

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL F 301

Chain	Residue
F	GLN37
F	PRO59
F	PHE62
F	GLU81
F	ASP82

---

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL F 302

Chain	Residue
F	GLN155
F	LEU181
F	HIS189
F	HOH459
F	HOH474
K	THR72

---

site_id	AC9
Number of Residues	11
Details	binding site for residue GOL F 303

Chain	Residue
E	PHE166
E	PRO167
E	VAL169
E	SER177
E	LEU178
E	SER179
E	HOH349
F	SER162
F	SER176
F	SER177
F	THR178

---

site_id	AD1
Number of Residues	7
Details	binding site for residue PO4 F 304

Chain	Residue
C	SER132
C	GLY133
F	LYS207
F	HOH404
F	HOH436
F	HOH448
F	HOH453

---

site_id	AD2
Number of Residues	2
Details	binding site for residue ACT F 305

Chain	Residue
F	ASP70
K	THR129

---

site_id	AD3
Number of Residues	10
Details	binding site for residue LDA F 306

Chain	Residue
F	ARG18
F	THR20
F	HOH424
G	SER53
G	THR73
G	GOL301
K	ALA153
K	GLN155
K	ASN158
K	HIS189

---

site_id	AD4
Number of Residues	2
Details	binding site for residue GOL F 307

Chain	Residue
F	ARG66
F	GLY68

---

site_id	AD5
Number of Residues	6
Details	binding site for residue GOL G 301

Chain	Residue
F	LDA306
G	SER52
G	SER53
G	GLY55
K	ASP151
K	ASN152

---

site_id	AD6
Number of Residues	3
Details	binding site for residue GOL H 301

Chain	Residue
H	SER161
K	ARG108
K	THR109

---

site_id	AD7
Number of Residues	10
Details	binding site for residue GOL H 302

Chain	Residue
H	PHE166
H	PRO167
H	VAL169
H	SER177
H	LEU178
H	SER179
L	GLN160
L	SER176
L	THR178
L	HOH407

---

site_id	AD8
Number of Residues	4
Details	binding site for residue GOL I 301

Chain	Residue
I	ALA112
I	SER114
I	ASN137
I	ASN138

---

site_id	AD9
Number of Residues	7
Details	binding site for residue GOL I 302

Chain	Residue
G	VAL163
G	HIS164
I	THR164
I	GLU165
I	ASP167
I	HOH419
I	HOH426

---

site_id	AE1
Number of Residues	10
Details	binding site for residue GOL I 303

Chain	Residue
G	PHE166
G	PRO167
G	VAL169
G	SER177
G	LEU178
G	SER179
I	GLN160
I	SER162
I	SER176
I	THR178

---

site_id	AE2
Number of Residues	2
Details	binding site for residue ACE J 301

Chain	Residue
J	LYS117
J	GLY118

---

site_id	AE3
Number of Residues	5
Details	binding site for residue GOL K 301

Chain	Residue
J	HIS164
K	GLU165
K	ASP167
K	HOH416
K	HOH445

---

site_id	AE4
Number of Residues	5
Details	binding site for residue GOL K 302

Chain	Residue
F	GLN199
K	HIS198
K	GLN199
K	LEU201
K	HOH444

---

site_id	AE5
Number of Residues	2
Details	binding site for residue GOL K 303

Chain	Residue
K	ALA112
K	GLY200

---

site_id	AE6
Number of Residues	10
Details	binding site for residue GOL L 301

Chain	Residue
H	PHE122
H	PRO123
H	LEU124
H	LEU141
L	PHE118
L	PRO119
L	PRO120
L	SER121
L	GLN124
L	SER131

---

site_id	AE7
Number of Residues	5
Details	binding site for residue GOL L 302

Chain	Residue
E	SER30
E	SER53
E	THR73
L	ARG18
L	SER76

---

site_id	AE8
Number of Residues	2
Details	binding site for residue ACE L 303

Chain	Residue
E	SER74
L	ARG61

---

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH

Chain	Residue	Details
B	TYR192-HIS198
A	TYR194-HIS200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66H76","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"26598620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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